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Conserved domains on  [gi|2462528239|ref|XP_054226232|]
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liprin-beta-2 isoform X6 [Homo sapiens]

Protein Classification

SAM_liprin-beta1,2_repeat2 and SAM_liprin-beta1,2_repeat3 domain-containing protein( domain architecture ID 10175983)

protein containing domains SAM_liprin-beta1,2_repeat1, SAM_liprin-beta1,2_repeat2, and SAM_liprin-beta1,2_repeat3

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 ...
 656-727 4.08e-44

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 153.38  E-value: 4.08e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 656 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 727
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 ...
 571-633 7.94e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 7.94e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 571 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 633
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 ...
 497-560 2.46e-35

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


:

Pssm-ID: 188962  Cd Length: 64  Bit Score: 128.11  E-value: 2.46e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 497 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 560
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-248 9.01e-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: 65.85  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   36 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 108
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  109 MTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 188
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239  189 HSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 248
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 656-727 4.08e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 153.38  E-value: 4.08e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 656 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 727
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 ...
 571-633 7.94e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 7.94e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 571 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 633
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 ...
 497-560 2.46e-35

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 128.11  E-value: 2.46e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 497 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 560
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 576-632 8.25e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 8.25e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 576 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 499-561 1.06e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 71.92  E-value: 1.06e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 499 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 561
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 497-561 4.82e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.71  E-value: 4.82e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239  497 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 561
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
657-727 5.67e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 5.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 657 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 727
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-248 9.01e-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: 65.85  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   36 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 108
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  109 MTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 188
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239  189 HSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 248
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 577-632 1.08e-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: 52.30  E-value: 1.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239  577 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-246 2.03e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  36 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 115
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 116 KLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT 195
Cdd:COG1196   336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 196 AALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 246
Cdd:COG1196   413 LERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 657-726 3.94e-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: 3.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  657 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 726
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 39-267 9.13e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.28  E-value: 9.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 118
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 193
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528239  194 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 267
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
137-286 3.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 137 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 207
Cdd:PRK03918  499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 208 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 285
Cdd:PRK03918  573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                  .
gi 2462528239 286 Q 286
Cdd:PRK03918  648 E 648
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 656-727 4.08e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 153.38  E-value: 4.08e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 656 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 727
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 ...
 571-633 7.94e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 7.94e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 571 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 633
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 ...
 497-560 2.46e-35

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 128.11  E-value: 2.46e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 497 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 560
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 ...
 664-725 1.97e-29

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 111.09  E-value: 1.97e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 664 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 725
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 ...
 656-727 3.54e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 110.61  E-value: 3.54e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 656 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 727
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 ...
 575-633 3.27e-28

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 107.62  E-value: 3.27e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 575 IWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 633
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 ...
 504-560 2.98e-26

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 101.92  E-value: 2.98e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239 504 RVCAWLEDFGLAQ-YVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 560
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 ...
 656-727 6.53e-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: 6.53e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 656 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 727
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 576-632 8.25e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 8.25e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 576 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 499-561 1.06e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 71.92  E-value: 1.06e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 499 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 561
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 ...
 571-633 4.23e-15

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 70.52  E-value: 4.23e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239 571 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 633
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 497-561 4.82e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.71  E-value: 4.82e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239  497 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 561
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 576-629 2.60e-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: 62.26  E-value: 2.60e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 576 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 629
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
657-727 5.67e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 5.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 657 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 727
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 504-559 1.13e-11

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 60.33  E-value: 1.13e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528239 504 RVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 559
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-248 9.01e-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: 65.85  E-value: 9.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   36 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 108
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  109 MTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 188
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239  189 HSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 248
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 572-632 9.85e-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: 55.17  E-value: 9.85e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 572 LDHIWV-TRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 632
Cdd:cd09565     1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 497-561 1.97e-09

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 54.49  E-value: 1.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 497 FAQWSTERVCAWLEDF-GL-AQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 561
Cdd:cd09562     1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 577-632 1.08e-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: 52.30  E-value: 1.08e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239  577 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-246 2.03e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  36 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 115
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 116 KLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT 195
Cdd:COG1196   336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 196 AALHSESHTERDQEIQRLKmgmETLLLANEDKDRRIEELTGLLNQYRKVKE 246
Cdd:COG1196   413 LERLERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAELEEEEEA 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-234 3.05e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 3.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   59 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEE 138
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  139 LLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAlkdaEIERLHSQLSRTAALHSESHTERDQEIQRLKMGME 218
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*.
gi 2462528239  219 TLLLANEDKDRRIEEL 234
Cdd:TIGR02168  828 SLERRIAATERRLEDL 843
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 657-726 3.94e-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: 3.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  657 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 726
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 498-558 7.39e-08

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 50.14  E-value: 7.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 498 AQWSTERVCAWLE-DFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 558
Cdd:cd09564     2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 39-267 9.13e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.28  E-value: 9.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 118
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 193
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528239  194 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 267
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
500-561 1.10e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 49.58  E-value: 1.10e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 500 WSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 561
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
137-249 1.91e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 54.86  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 137 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 214
Cdd:COG2433   409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462528239 215 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 249
Cdd:COG2433   472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-256 2.11e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  10 RGGQRLGSRRTVKATSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEvcleghqVKLNAAEE 89
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLEERRRE-LEERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEA 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  90 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEwklkatkA 169
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELEELAEEL----------LEALRAAAELAAQLEELEEAEEALLERLERLE-------E 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 170 EVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 249
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                  ....*..
gi 2462528239 250 VTQGPSE 256
Cdd:COG1196   502 DYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-242 3.89e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  39 QERLARLEgDKES-LILQVSVLTDQVEA--------QGEKIRDLEVCLeghqVKLNAAEEMLQQELLSRTSLETQKLDLM 109
Cdd:COG1196   185 EENLERLE-DILGeLERQLEPLERQAEKaeryrelkEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 110 TEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 189
Cdd:COG1196   260 AELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 190 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 242
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 500-569 6.12e-07

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 47.70  E-value: 6.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 500 WSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 569
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-240 8.10e-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: 52.07  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDL---------M 109
Cdd:COG4942    40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 110 TEVSELKLKLvgmekeqreqeekqrKAEELLQELRHLKIkVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 189
Cdd:COG4942   117 GRQPPLALLL---------------SPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 190 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQ 240
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-246 1.27e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239    4 STVMADRGGQRLGSRRTV--KATSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ 81
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLleELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   82 VKLNAAEEMLQQELLSRTSLetqkldlMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYE 161
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKL-------TEEYAELKEEL----------EDLRAELEEVDKEFAETRDELKDYREKLEKLK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  162 WKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQY 241
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478


                   ....*
gi 2462528239  242 RKVKE 246
Cdd:TIGR02169  479 DRVEK 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-234 1.57e-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: 51.98  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 118
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 LVGMEKEQREQEEKQRKAEELLQ-----------ELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIER 187
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462528239  188 LHSQLSRTAALHSESHTERD---QEIQRLKMGMETLLLANEDKDRRIEEL 234
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEallNERASLEEALALLRSELEELSEELREL 906
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 500-556 1.75e-06

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 46.17  E-value: 1.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 500 WSTERVCAWLEDF-GLAQYVIFARQWVSSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 556
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 496-559 2.48e-06

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 45.48  E-value: 2.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239 496 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 559
Cdd:cd09507     1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 35-267 4.08e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  35 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 109
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 110 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvaLKDAEIErlh 189
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE--LKKENLE--- 560

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239 190 sqlsrtaalhsESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPE 267
Cdd:TIGR04523 561 -----------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
577-629 6.79e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 6.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 577 VTRWLDDIGLPQYKDQFHESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 629
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 577-630 8.58e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 43.84  E-value: 8.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 577 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 630
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
36-208 9.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 9.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   36 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSE 114
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAA 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  115 LKLKLVGmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSR 194
Cdd:COG4913    371 LGLPLPA-------------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437

                          170
                   ....*....|....
gi 2462528239  195 taaLHSESHTERDQ 208
Cdd:COG4913    438 ---IPARLLALRDA 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 134-246 1.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 134 RKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRL 213
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462528239 214 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 246
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEA 358
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 574-632 1.63e-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: 1.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 574 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:cd09506     3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
8-287 1.83e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   8 ADRGGQRLGSRR--TVKATSQVNHHSAASNETYQERLARLEgdkeSLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLN 85
Cdd:COG4372     1 GDRLGEKVGKARlsLFGLRPKTGILIAALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  86 AAEEMLQQellSRTSLETQKLDLMTEVSELklklvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLK 165
Cdd:COG4372    77 QLEEELEE---LNEQLQAAQAELAQAQEEL---------------------ESLQEEAEELQEELEELQKERQDLEQQRK 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 166 ATKAEVAQLQEQVALKDAEIERLHSQLsrtaalhseshTERDQEIQRLKMGMETLLLAN---------EDKDRRIEELTG 236
Cdd:COG4372   133 QLEAQIAELQSEIAEREEELKELEEQL-----------ESLQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEE 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 237 LLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFSKWNATNKDPEELFKQE 287
Cdd:COG4372   202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 501-554 1.86e-05

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 43.02  E-value: 1.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 501 STERVCAWLEDFGLAQYvifARQWVSSGHTLLT---ATPQDMeKELGIKHPLHRKKL 554
Cdd:cd09497     3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 577-632 1.98e-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: 1.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528239 577 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:cd09530     8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 18-248 2.51e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   18 RRTVKATSQ-VNHHSAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAEE 89
Cdd:pfam15921  568 RQQIENMTQlVGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELEARvsdLELEKVKLvNAGSE 643

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   90 MLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQreqeekqrkaeELLQelRHLKIKVEELENERNQYEWKLKATKA 169
Cdd:pfam15921  644 RLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKSEEMETTTNKLKMQLKSAQS 706

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  170 EVAQ---------------------LQEQVALKDAEIERLHSQLSrtaaLHSESHTERDQEIQRL-----KMGMETLLLA 223
Cdd:pfam15921  707 ELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQ----FLEEAMTNANKEKHFLkeeknKLSQELSTVA 782

                          250       260
                   ....*....|....*....|....*
gi 2462528239  224 NEdKDRRIEELTGLLNQYRKVKEIV 248
Cdd:pfam15921  783 TE-KNKMAGELEVLRSQERRLKEKV 806
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-191 2.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVS 113
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239 114 ELKLKLVgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 191
Cdd:COG4717   174 ELQEELE---------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 36-236 3.59e-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: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  36 ETYQERLarleGDKESlilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLsRTSLETQKlDLMTEVS 113
Cdd:pfam05483 229 EEYKKEI----NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDENL-KELIEKKD-HLTKELE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 114 ELKLKLVGMEKEQREQEEKQRKAEELLQELRHLK-IKVEELENERNQYEWKLKATKAEVAQLQE--------------QV 178
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAAHSFVVTEFEATTCSLEEllrteqqrleknedQL 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239 179 ALKDAEIERLHSQLSRTAALHSESHTERdQEIQRLKMGMETLLLANEDKDRRIEELTG 236
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKG 436
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 44-245 4.01e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   44 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 123
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  124 KEQREQEEKQRKAEEllqELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDA--------------EIERLH 189
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239  190 SQLSRT---AALHSESHTERDQEIQRLKMGMETLLLANEDK--DRR------IEELTGLLNQYRKVK 245
Cdd:pfam01576  306 TELEDTldtTAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNK 372
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 17-234 4.49e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   17 SRRTVKATSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTD--------QVEAQGEKI-----------RDLEVCL 77
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripEIQAELSKLeeevsriearlREIEQKL 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   78 EGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQrkaEELLQELRHLKIKVEELENER 157
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL---RDLESRLGDLKKERDELEAQL 898

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239  158 NQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSrtaalHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEEL 234
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 38-269 4.51e-05

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 46.29  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  38 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRT---SLETQKLDLMTEVSE 114
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLREeiqKLRGQIQQLRTELQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 115 LKLKLVgmeKEQREQEEKQRKAEELLQELRHLKikvEELENERNQYEWKLKATKAEV----AQLQEQVALKDAEIERLHS 190
Cdd:pfam09787  80 LEAQQQ---EEAESSREQLQELEEQLATERSAR---REAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 191 QLSrtaaLHSESHTERDQEIQRLKMGMETLLlaneDKDRRIEELT----GLLNQYRKVKEIVMVTQGPSERTLSINEEEP 266
Cdd:pfam09787 154 QLT----SKSQSSSSQSELENRLHQLTETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGI 225


                  ...
gi 2462528239 267 EGG 269
Cdd:pfam09787 226 SDG 228
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 498-559 4.87e-05

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 42.24  E-value: 4.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462528239 498 AQWSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 559
Cdd:cd09515     2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 505-558 6.03e-05

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 41.63  E-value: 6.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239 505 VC-AWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 558
Cdd:cd09567     7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 36-233 6.16e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  36 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 115
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 116 KLKLvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQyEWkLKATKAEVAQLQEQvalkdaeIERLHSQLSRT 195
Cdd:TIGR04523 280 NKKI-----------------KELEKQLNQLKSEISDLNNQKEQ-DW-NKELKSELKNQEKK-------LEEIQNQISQN 333

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462528239 196 aalhSESHTERDQEIQRLKMGMETLLLANEDKDRRIEE 233
Cdd:TIGR04523 334 ----NKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 574-630 7.54e-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: 41.55  E-value: 7.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 574 HIW----VTRWL-DDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 630
Cdd:cd09504     3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-197 8.16e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 8.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLM 109
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  110 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQV-ALKDaeIERL 188
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQEN 500


                   ....*....
gi 2462528239  189 HSQLSRTAA 197
Cdd:TIGR02168  501 LEGFSEGVK 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 77-248 9.65e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 9.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   77 LEGHQVKLNAAEEMLQQELlsrTSLETQKLDLMTEVSELKlklvgmekeqreqeekqRKAEELLQELRHLKIKVEELENE 156
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIE-----------------NRLDELSQELSDASRKIGEIEKE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  157 RNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhseshterdqEIQRLKMGMETLLLANEDKDRRI--EEL 234
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-----------RIEELEEDLHKLEEALNDLEARLshSRI 793

                          170
                   ....*....|....
gi 2462528239  235 TGLLNQYRKVKEIV 248
Cdd:TIGR02169  794 PEIQAELSKLEEEV 807
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-197 1.19e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  36 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 93
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  94 ---ELLSR----TSLETQKLDLMTEVSELKLKLvgmekeQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKA 166
Cdd:COG3883   113 sfsDFLDRlsalSKIADADADLLEELKADKAEL------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462528239 167 TKAEVAQLQEQVALKDAEIERLHSQLSRTAA 197
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 138-246 1.76e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 138 ELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERdqEIQRLKMGM 217
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQKEI 98

                          90       100
                  ....*....|....*....|....*....
gi 2462528239 218 ETLLLANEDKDRRIEELTGLLNQYRKVKE 246
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELA 127
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
13-220 1.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  13 QRLGSRRTVKATSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQ 92
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  93 QeLLSRTSLET------------QKLDLMTEVSELKLKLVGmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQY 160
Cdd:COG4717   374 A-LLAEAGVEDeeelraaleqaeEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 161 EWKLKATKAEVAQLQEQVAL--KDAEIERLHSQLSRTAalhseshterdQEIQRLKMGMETL 220
Cdd:COG4717   452 REELAELEAELEQLEEDGELaeLLQELEELKAELRELA-----------EEWAALKLALELL 502
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-214 2.39e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   18 RRTVKATSQVNH--HSAASNETYQERLARLEgDKESLILQVSVLTDQ--VEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ 93
Cdd:COG4913    242 EALEDAREQIELlePIRELAERYAAARERLA-ELEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   94 ELLSRTSLETQKLDLMTEvselklklvgmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYE-------WKLKA 166
Cdd:COG4913    321 LREELDELEAQIRGNGGD-----------------------RLEQLEREIERLERELEERERRRARLEallaalgLPLPA 377

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462528239  167 TKAEVAQLQEQVAL----KDAEIERLHSQLSRTAALHSES---HTERDQEIQRLK 214
Cdd:COG4913    378 SAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDLrreLRELEAEIASLE 432
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 496-561 3.25e-04

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 39.55  E-value: 3.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 496 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 561
Cdd:cd09575     1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-246 4.69e-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: 43.89  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLEVCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSElklk 118
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEE---- 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 lvgmekeqreqeeKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA- 197
Cdd:TIGR02168  258 -------------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAq 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239  198 -LHSESHTERDQE--------IQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 246
Cdd:TIGR02168  325 lEELESKLDELAEelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 41-92 7.56e-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: 39.43  E-value: 7.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462528239  41 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 92
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 136-197 8.44e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 8.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462528239 136 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 197
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
40-238 8.66e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  40 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 116
Cdd:COG4717    71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 117 LKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLK-ATKAEVAQLQEQVALKDAEIERLHSQLSRT 195
Cdd:COG4717   139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEA 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462528239 196 aalhSESHTERDQEIQRLKMGMETlllanEDKDRRIEELTGLL 238
Cdd:COG4717   219 ----QEELEELEEELEQLENELEA-----AALEERLKEARLLL 252
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 12-246 1.12e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  12 GQRLGSRRTVKATSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG-------HQVKL 84
Cdd:pfam07888  73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTltqrvleRETEL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  85 NAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKL 164
Cdd:pfam07888 153 ERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 165 KATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQeiQRLKMGMETLLLAN------EDKDRRIEELTGLL 238
Cdd:pfam07888 233 EALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQLADaslalrEGRARWAQERETLQ 310


                  ....*...
gi 2462528239 239 NQYRKVKE 246
Cdd:pfam07888 311 QSAEADKD 318
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 577-611 1.90e-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: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462528239 577 VTRWLDDIGLPQYKDQF-HESRVDGRMLQYLTVNDL 611
Cdd:cd09515     9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 494-545 2.40e-03

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 37.25  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 494 NAPFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGI 545
Cdd:cd09512     1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 51-240 2.54e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  51 SLILQVSVLTDQVEAqgeKIRDLEVCLEGHQVKLNAAEEMLQQEllsrtsletqkldlMTEVSELKLKLVGMEKEQREQE 130
Cdd:pfam15905 156 SLSMELMKLRNKLEA---KMKEVMAKQEGMEGKLQVTQKNLEHS--------------KGKVAQLEEKLVSTEKEKIEEK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 131 EKQrkaEELLQElrhlkikVEELENERNQYEwklkATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEI 210
Cdd:pfam15905 219 SET---EKLLEY-------ITELSCVSEQVE----KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462528239 211 QRLKMGMETLLLANEDKDRR----IEELTGLLNQ 240
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTlnaeLEELKEKLTL 318
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-246 3.00e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELklk 118
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL--- 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 lvgmekeqreqeekqrkaEELLQELRHlkikveelenERNQYEWKLKATKAEVAQLQEQVAlkdaeierlhSQLSRTAAL 198
Cdd:TIGR02168  914 ------------------RRELEELRE----------KLAQLELRLEGLEVRIDNLQERLS----------EEYSLTLEE 955

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462528239  199 HSESHTERDQEIQRLKmgmetlllanedkdRRIEELTGLLNQ-----------YRKVKE 246
Cdd:TIGR02168  956 AEALENKIEDDEEEAR--------------RRLKRLENKIKElgpvnlaaieeYEELKE 1000
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 36-242 3.12e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   36 ETYQERLARLEGDKESL----ILQVSVLTDQVEAQGEKIRDLEVCLEGHQVK-LNAAEEMLQQELLSRTSLETQKLDLMT 110
Cdd:TIGR00618  639 QELALKLTALHALQLTLtqerVREHALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIEEYDR 718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  111 EVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHL---KIKVEELENER-NQYEWKLKATKAEVAQLQEQVALKDAEIE 186
Cdd:TIGR00618  719 EFNEIENAS---SSLGSDLAAREDALNQSLKELMHQartVLKARTEAHFNnNEEVTAALQTGAELSHLAAEIQFFNRLRE 795

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528239  187 RLHSQLsrtAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 242
Cdd:TIGR00618  796 EDTHLL---KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-240 3.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  141 QELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETL 220
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQL 752

                           90       100
                   ....*....|....*....|
gi 2462528239  221 LLANEDKDRRIEELTGLLNQ 240
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEE 772
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
137-286 3.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 137 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 207
Cdd:PRK03918  499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 208 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 285
Cdd:PRK03918  573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                  .
gi 2462528239 286 Q 286
Cdd:PRK03918  648 E 648
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-247 3.86e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  61 DQVEAQGEKIRDLEvcleghqvklnAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqreqeekqrkaeELL 140
Cdd:COG4717    71 KELKELEEELKEAE-----------EKEEEYAELQEELEELEEELEELEAELEELREELEKL---------------EKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 141 QELRHLKIKVEELENERNQYEWK---LKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTER----DQEIQRL 213
Cdd:COG4717   125 LQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEEL 204

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462528239 214 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 247
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 41-246 4.24e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  41 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlMTEVSELKlklv 120
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNK---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 121 gmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhs 200
Cdd:COG1579    90 --------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA--- 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 201 eshtERDQEIQRLKmgmetlllanedkdRRIEELTG-----LLNQYRKVKE 246
Cdd:COG1579   153 ----ELEAELEELE--------------AEREELAAkippeLLALYERIRK 185
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 498-546 4.68e-03

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 36.50  E-value: 4.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 498 AQWSTERVCAWLE--DFGLAQYVIFARQWVSSGHTLLTATPQDMEkELGIK 546
Cdd:cd09511     2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 137-243 4.82e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 137 EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT----AALHSESHTERDQEIQR 212
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAELEAQKEELAEL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462528239 213 L----KMGME---TLLLANEDKDR--RIEELTGLLNQYRK 243
Cdd:COG4942   110 LralyRLGRQpplALLLSPEDFLDavRRLQYLKYLAPARR 149
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 574-632 4.92e-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: 36.47  E-value: 4.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528239 574 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 632
Cdd:cd09575     3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 574-621 6.48e-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: 36.12  E-value: 6.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 574 HIWVT----RWLDD-IGLPQYKDQFHESRVDGRMLQYLTVNDLLF----LKVTSQLH 621
Cdd:cd09574     3 HNWTMedtlQWLKEfVELPQYEKNFRDNNVKGTTLPRIAVNEPSFmisqLKILDRSH 59
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 39-178 7.02e-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: 39.14  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  39 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 102
Cdd:COG1579    30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 103 TQKLDLMTEVSELKLKLvgmekeqreqeekqRKAEELLQELR-HLKIKVEELENERNQYEWKLKATKAEVAQLQEQV 178
Cdd:COG1579   110 DEILELMERIEELEEEL--------------AELEAELAELEaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-247 7.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 136 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALH---------SESHTER 206
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklSEFYEEY 305

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 207 DQEIQRLKMGMETL--LLAN--------EDKDRRIEELTGLLNQYRKVKEI 247
Cdd:PRK03918  306 LDELREIEKRLSRLeeEINGieerikelEEKEERLEELKKKLKELEKRLEE 356
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 508-562 7.05e-03

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


Pssm-ID: 188897  Cd Length: 71  Bit Score: 36.12  E-value: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528239 508 WLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMEkELGIKHPLHRKKLVLAVKAIN 562
Cdd:cd09498    13 WLSLLGLPQYHkVLVENGYDSIDFVTDLTWEDLQ-DIGITKLGHQKKLMLAIKKLK 67
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 577-611 7.30e-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: 35.74  E-value: 7.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462528239 577 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL 611
Cdd:cd09501     9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDEL 43
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 40-288 8.40e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239   40 ERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ-VKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 118
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  119 LV----GMEKEQREqeekqrkAEELLQELRHLKIKVEELENERNQYEwklKATKAEVAQLQEQVALKDAEIERLHSQLSR 194
Cdd:pfam02463  323 KKkaekELKKEKEE-------IEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKL 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  195 TAALHSESHT---ERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPEGGFS 271
Cdd:pfam02463  393 KEEELELKSEeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472

                          250
                   ....*....|....*..
gi 2462528239  272 KWNATNKDPEELFKQEM 288
Cdd:pfam02463  473 LLKETQLVKLQEQLELL 489
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 500-545 8.73e-03

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


Pssm-ID: 188934  Cd Length: 65  Bit Score: 35.61  E-value: 8.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462528239 500 WSTERVCAWLEDFGLAQYVI--FARQWVsSGHTLLTATPQDMeKELGI 545
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSVCekFRENEI-TGDILLELDLEDL-KELDI 48
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 136-192 8.95e-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: 37.21  E-value: 8.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528239 136 AEELLQELRHLKIKVEElenERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQL 192
Cdd:pfam20492  60 AEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 25-259 9.02e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  25 SQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRTSLETQ 104
Cdd:pfam05557  58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239 105 KLDLMTEVSELKLKLVGMEKEQREQeekqrkaEELLQELRHLKIKVEELENERNQYE-WK--LKATKAEVAQLQEQvalk 181
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDSeiVKNSKSELARIPEL---- 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528239 182 DAEIERLHSqlsrtaalhseshterdqEIQRLKMGMETLLLANEDKdrriEELTGLLNQYRKVKEIVMVTQGPSERTL 259
Cdd:pfam05557 203 EKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLKRKLEREEKYREEAATLELEKEKLE 258
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
 15-237 9.62e-03

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


Pssm-ID: 463001  Cd Length: 523  Bit Score: 39.42  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  15 LGSRRTVKATSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQE 94
Cdd:pfam10212 291 LSNRRVLLSSTESREGLAQQVQQSQEKIAKLEQEKEHWMLEAQLLKIKLEKENQRIADLEKQLLKGSTSGQLPELVQSKA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528239  95 LLSRTSLETQKLDLMTEVSELK-LKLVGMEKEQREQEEK--QRKAEELLQElrHLKIKVEELENERNQYEWKLKATKAEV 171
Cdd:pfam10212 371 TLPLTAKQGSEASSISEKEPTPsTSLIGMLTVTTDSEESsdEESREQLIKS--HYMARIAELTSQLQLADSKAVHFHAEC 448

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462528239 172 AQLQEQVALKDAEIERLHSQL----SRTAALHSE-SHTERDQEIQrLKMGMETLLLANEDKDRRIEELTGL 237
Cdd:pfam10212 449 RALAKRLALAEKSKESLTEELklanQNISRLQDElTTTKRSYEDQ-LSMMSDHLCSMNETLTKQREEIDTL 518
 
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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