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Conserved domains on  [gi|1844083926|ref|NP_001338786|]
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liprin-beta-2 isoform 8 [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 ...
 648-719 3.91e-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: 3.91e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 648 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 719
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 ...
 563-625 9.96e-37

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 132.05  E-value: 9.96e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 563 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 625
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 ...
 489-552 2.93e-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: 127.73  E-value: 2.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 489 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 552
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-240 7.01e-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: 66.23  E-value: 7.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   14 LKRSQVNHHSAASN-ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTS 92
Cdd:TIGR02168  248 LKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   93 LETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAL 172
Cdd:TIGR02168  328 LESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  173 KDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 240
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 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 ...
 648-719 3.91e-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: 3.91e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 648 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 719
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 ...
 563-625 9.96e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 132.05  E-value: 9.96e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 563 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 625
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 ...
 489-552 2.93e-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: 127.73  E-value: 2.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 489 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 552
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 491-553 1.37e-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: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 491 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 553
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-624 2.55e-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: 71.15  E-value: 2.55e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 568 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 489-553 6.21e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.32  E-value: 6.21e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926  489 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 553
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
649-719 6.57e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 649 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 719
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-240 7.01e-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: 66.23  E-value: 7.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   14 LKRSQVNHHSAASN-ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTS 92
Cdd:TIGR02168  248 LKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   93 LETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAL 172
Cdd:TIGR02168  328 LESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  173 KDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 240
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 466
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 649-718 4.84e-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: 50.37  E-value: 4.84e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  649 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 718
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 569-624 8.70e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 8.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926  569 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-259 8.78e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.28  E-value: 8.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 110
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 185
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  186 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 259
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-238 1.48e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  28 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG-------HQVKLNAAEEMLQQELLSRTSLETQKLDL 100
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 101 MTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 180
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 181 HSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
129-278 4.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 129 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 199
Cdd:PRK03918  499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 200 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 277
Cdd:PRK03918  573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                  .
gi 1844083926 278 Q 278
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 ...
 648-719 3.91e-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: 3.91e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 648 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 719
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 ...
 563-625 9.96e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 132.05  E-value: 9.96e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 563 LLDHIWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 625
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 ...
 489-552 2.93e-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: 127.73  E-value: 2.93e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 489 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 552
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 ...
 656-717 1.84e-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: 1.84e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 656 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 717
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 ...
 648-719 3.51e-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: 3.51e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 648 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 719
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 ...
 567-625 4.64e-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: 107.23  E-value: 4.64e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 567 IWVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 625
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 ...
 496-552 2.63e-26

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 102.30  E-value: 2.63e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 496 RVCAWLEDFGLAQ-YVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 552
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 ...
 648-719 6.85e-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: 6.85e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 648 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 719
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 491-553 1.37e-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: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 491 QWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 553
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 568-624 2.55e-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: 71.15  E-value: 2.55e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 568 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 489-553 6.21e-14

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 67.32  E-value: 6.21e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926  489 FAQWSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 553
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 563-625 8.14e-14

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 66.66  E-value: 8.14e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926 563 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 625
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
649-719 6.57e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 649 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 719
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 496-551 1.40e-11

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 59.95  E-value: 1.40e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083926 496 RVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 551
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 568-621 2.07e-11

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 59.56  E-value: 2.07e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 568 WVTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 621
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-240 7.01e-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: 66.23  E-value: 7.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   14 LKRSQVNHHSAASN-ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTS 92
Cdd:TIGR02168  248 LKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   93 LETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAL 172
Cdd:TIGR02168  328 LESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  173 KDAEIERLHSQLSRTAALHSESHTERDQEIQRLKMG-METLLLANEDKDRRIEELTGLLNQYRKVKEIV 240
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEEL 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 ...
 564-624 1.77e-09

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 54.40  E-value: 1.77e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 564 LDHIWV-TRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 624
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 ...
 489-553 1.95e-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: 1.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 489 FAQWSTERVCAWLEDF-GL-AQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 553
Cdd:cd09562     1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-226 3.06e-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: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   51 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEE 130
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  131 LLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVAlkdaEIERLHSQLSRTAALHSESHTERDQEIQRLKMGME 210
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----QLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                          170
                   ....*....|....*.
gi 1844083926  211 TLLLANEDKDRRIEEL 226
Cdd:TIGR02168  828 SLERRIAATERRLEDL 843
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 649-718 4.84e-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: 50.37  E-value: 4.84e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  649 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 718
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 ...
 490-550 6.90e-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: 6.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 490 AQWSTERVCAWLE-DFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 550
Cdd:cd09564     2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 569-624 8.70e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.60  E-value: 8.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926  569 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-259 8.78e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 56.28  E-value: 8.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 110
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 LvgmekeqreqeekqrkaEELLQELRHLKIKVEELENernqyewklkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 185
Cdd:pfam15921  526 V-----------------DLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  186 -----RTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYrKVKEIVMVTQGpSERTLSINEEEPE 259
Cdd:pfam15921  578 vgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL-ELEKVKLVNAG-SERLRAVKDIKQE 654
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
492-553 1.27e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 49.19  E-value: 1.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 492 WSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 553
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-238 1.48e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  28 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG-------HQVKLNAAEEMLQQELLSRTSLETQKLDL 100
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 101 MTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 180
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 181 HSQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
129-241 1.98e-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: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 129 EELLQELRHLKIKVEELEnernqyewklkatkAEVAQLQEQVALKDAEIERLHSQLSRtaaLHSESHTE--RDQEIQRLK 206
Cdd:COG2433   409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSE---ARSEERREirKDREISRLD 471

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844083926 207 MGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVM 241
Cdd:COG2433   472 REIERLERELEEERERIEELKRKLERLKELWKLEH 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-234 3.53e-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: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  31 QERLARLEgDKES-LILQVSVLTDQVEA--------QGEKIRDLEVCLeghqVKLNAAEEMLQQELLSRTSLETQKLDLM 101
Cdd:COG1196   185 EENLERLE-DILGeLERQLEPLERQAEKaeryrelkEELKELEAELLL----LKLRELEAELEELEAELEELEAELEELE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 102 TEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 181
Cdd:COG1196   260 AELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 182 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 234
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-248 5.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  22 HSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLM 101
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAE 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 102 TEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEwklkatkAEVAQLQEQVALKDAEIERLH 181
Cdd:COG1196   379 EELEELAEEL----------LEALRAAAELAAQLEELEEAEEALLERLERLE-------EELEELEEALAELEEEEEEEE 441

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 182 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSE 248
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 31-232 6.21e-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: 52.46  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDL---------M 101
Cdd:COG4942    40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 102 TEVSELKLKLvgmekeqreqeekqrKAEELLQELRHLKIkVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLH 181
Cdd:COG4942   117 GRQPPLALLL---------------SPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 182 SQLSRTAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQ 232
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 492-561 6.62e-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: 47.31  E-value: 6.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 492 WSTERVCAWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 561
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-226 1.53e-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: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 110
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 LVGMEKEQREQEEKQRKAEELLQ-----------ELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIER 179
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1844083926  180 LHSQLSRTAALHSESHTERD---QEIQRLKMGMETLLLANEDKDRRIEEL 226
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEallNERASLEEALALLRSELEELSEELREL 906
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 31-238 1.81e-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: 51.99  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLetqkldlMTEVSELKLK 110
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL-------TEEYAELKEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 LvgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAL 190
Cdd:TIGR02169  366 L----------EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1844083926  191 HSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 492-548 1.89e-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: 1.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 492 WSTERVCAWLEDF-GLAQYVIFARQWVSSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 548
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 488-551 2.65e-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: 2.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926 488 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 551
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 ...
 27-259 6.34e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  27 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 101
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 102 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQvaLKDAEIErlh 181
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE--LKKENLE--- 560

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 182 sqlsrtaalhsESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEEEPE 259
Cdd:TIGR04523 561 -----------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-200 9.14e-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: 9.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   28 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSE 106
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAA 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  107 LKLKLVGmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSR 186
Cdd:COG4913    371 LGLPLPA-------------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437

                          170
                   ....*....|....
gi 1844083926  187 taaLHSESHTERDQ 200
Cdd:COG4913    438 ---IPARLLALRDA 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 126-238 1.08e-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: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 126 RKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEIQRL 205
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1844083926 206 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEA 358
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 493-546 2.22e-05

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 43.02  E-value: 2.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 493 STERVCAWLEDFGLAQYvifARQWVSSGHTLLT---ATPQDMeKELGIKHPLHRKKL 546
Cdd:cd09497     3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
24-279 2.33e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  24 AASNETYQERLARLEgdkeSLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDLMTE 103
Cdd:COG4372    27 AALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 104 VSELklklvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 183
Cdd:COG4372   100 QEEL---------------------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 184 LsrtaalhseshTERDQEIQRLKMGMETLLLAN---------EDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSIN 254
Cdd:COG4372   159 L-----------ESLQEELAALEQELQALSEAEaeqaldellKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227

                         250       260
                  ....*....|....*....|....*
gi 1844083926 255 EEEPEGGFSKWNATNKDPEELFKQE 279
Cdd:COG4372   228 EAKLGLALSALLDALELEEDKEELL 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
31-183 2.59e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVS 105
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 106 ELKLKLVgmekeqreqEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQ 183
Cdd:COG4717   174 ELQEELE---------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 30-261 3.70e-05

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 46.67  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  30 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRT---SLETQKLDLMTEVSE 106
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLREeiqKLRGQIQQLRTELQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 107 LKLKLVgmeKEQREQEEKQRKAEELLQELRHLKikvEELENERNQYEWKLKATKAEV----AQLQEQVALKDAEIERLHS 182
Cdd:pfam09787  80 LEAQQQ---EEAESSREQLQELEEQLATERSAR---REAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 183 QLSrtaaLHSESHTERDQEIQRLKMGMETLLlaneDKDRRIEELT----GLLNQYRKVKEIVMVTQGPSERTLSINEEEP 258
Cdd:pfam09787 154 QLT----SKSQSSSSQSELENRLHQLTETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGI 225


                  ...
gi 1844083926 259 EGG 261
Cdd:pfam09787 226 SDG 228
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 36-237 3.86e-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: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   36 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 115
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  116 KEQREQEEKQRKAEEllqELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDA--------------EIERLH 181
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926  182 SQLSRT---AALHSESHTERDQEIQRLKMGMETLLLANEDK--DRR------IEELTGLLNQYRKVK 237
Cdd:pfam01576  306 TELEDTldtTAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNK 372
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
569-621 4.38e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.26  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 569 VTRWLDDIGLPQYKDQFHESRVD-RRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 621
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKI 62
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 19-240 4.46e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   19 VNHHSAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLEVC---LEGHQVKL-NAAEEMLQqellSRT 91
Cdd:pfam15921  578 VGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELEARvsdLELEKVKLvNAGSERLR----AVK 649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   92 SLETQKLDLMTEVSELKLKLVGMEKEQreqeekqrkaeELLQelRHLKIKVEELENERNQYEWKLKATKAEVAQ------ 165
Cdd:pfam15921  650 DIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlk 716

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  166 ---------------LQEQVALKDAEIERLHSQLSrtaaLHSESHTERDQEIQRL-----KMGMETLLLANEdKDRRIEE 225
Cdd:pfam15921  717 smegsdghamkvamgMQKQITAKRGQIDALQSKIQ----FLEEAMTNANKEKHFLkeeknKLSQELSTVATE-KNKMAGE 791

                          250
                   ....*....|....*
gi 1844083926  226 LTGLLNQYRKVKEIV 240
Cdd:pfam15921  792 LEVLRSQERRLKEKV 806
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-226 4.59e-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: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   30 YQERLARLEGD-KESLILQVSVLTDQVEAQGEKI----RDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEV 104
Cdd:TIGR02169  777 LEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIearlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  105 SELKLKLVGMEKEQREQEEKQrkaEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQL 184
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1844083926  185 SrtaalHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEEL 226
Cdd:TIGR02169  934 S-----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 28-228 4.70e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  28 ETYQERLarleGDKESlilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLSRtsLETQKLDLMTEVS 105
Cdd:pfam05483 229 EEYKKEI----NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 106 ELKLKLVGMEKEQREQEEKQRKAEELLQELRHLK-IKVEELENERNQYEWKLKATKAEVAQLQE--------------QV 170
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAAHSFVVTEFEATTCSLEEllrteqqrleknedQL 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 171 ALKDAEIERLHSQLSRTAALHSESHTERdQEIQRLKMGMETLLLANEDKDRRIEELTG 228
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKG 436
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 490-551 5.93e-05

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 41.85  E-value: 5.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 490 AQWSTERVCAWLEDFGLAQYV-IFARQWVSSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 551
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 ...
 497-550 6.65e-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: 6.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926 497 VC-AWLEDFGLAQYVIFARQWVSSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 550
Cdd:cd09567     7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 28-189 7.63e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 7.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  28 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 85
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  86 ---ELLSRTS----LETQKLDLMTEVSELKLKLvgmekeqreqEEKQRKAEELLQELRHLKIKVE----ELENERNQYEW 154
Cdd:COG3883   113 sfsDFLDRLSalskIADADADLLEELKADKAEL----------EAKKAELEAKLAELEALKAELEaakaELEAQQAEQEA 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1844083926 155 KLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 189
Cdd:COG3883   183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-189 8.63e-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: 8.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLM 101
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQE 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  102 TEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQV-ALKDaeIERL 180
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQEN 500


                   ....*....
gi 1844083926  181 HSQLSRTAA 189
Cdd:TIGR02168  501 LEGFSEGVK 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 69-240 1.01e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   69 LEGHQVKLNAAEEMLQQELlsrTSLETQKLDLMTEVSELKlklvgmekeqreqeekqRKAEELLQELRHLKIKVEELENE 148
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERL---EGLKRELSSLQSELRRIE-----------------NRLDELSQELSDASRKIGEIEKE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  149 RNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhseshterdqEIQRLKMGMETLLLANEDKDRRI--EEL 226
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-----------RIEELEEDLHKLEEALNDLEARLshSRI 793

                          170
                   ....*....|....
gi 1844083926  227 TGLLNQYRKVKEIV 240
Cdd:TIGR02169  794 PEIQAELSKLEEEV 807
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 28-225 1.06e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  28 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 107
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 108 KLKLvgmekeqreqeekqrkaEELLQELRHLKIKVEELENERNQyEWkLKATKAEVAQLQEQvalkdaeIERLHSQLSRT 187
Cdd:TIGR04523 280 NKKI-----------------KELEKQLNQLKSEISDLNNQKEQ-DW-NKELKSELKNQEKK-------LEEIQNQISQN 333

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1844083926 188 aalhSESHTERDQEIQRLKMGMETLLLANEDKDRRIEE 225
Cdd:TIGR04523 334 ----NKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 130-238 1.83e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 130 ELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERdqEIQRLKMGM 209
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQKEI 98

                          90       100
                  ....*....|....*....|....*....
gi 1844083926 210 ETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELA 127
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 569-622 2.60e-04

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 39.61  E-value: 2.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 569 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 622
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 488-553 3.52e-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: 3.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 488 PFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 553
Cdd:cd09575     1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 566-624 4.14e-04

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 39.22  E-value: 4.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 566 HIW----VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:cd09506     3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-206 4.59e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   25 ASNETYQERLARLEgDKESLILQVSVLTDQ--VEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMT 102
Cdd:COG4913    259 ELAERYAAARERLA-ELEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  103 EvselklklvgmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYE-------WKLKATKAEVAQLQEQVAL--- 172
Cdd:COG4913    338 D-----------------------RLEQLEREIERLERELEERERRRARLEallaalgLPLPASAEEFAALRAEAAAlle 394

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1844083926  173 -KDAEIERLHSQLSRTAALHSES---HTERDQEIQRLK 206
Cdd:COG4913    395 aLEEELEALEEALAEAEAALRDLrreLRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-238 4.63e-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: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLEVCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSElklk 110
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEE---- 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 lvgmekeqreqeeKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA- 189
Cdd:TIGR02168  258 -------------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAq 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926  190 -LHSESHTERDQE--------IQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKE 238
Cdd:TIGR02168  325 lEELESKLDELAEelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 569-624 5.87e-04

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 38.84  E-value: 5.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083926 569 VTRWLDDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 624
Cdd:cd09530     8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 128-189 6.32e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 6.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083926 128 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAA 189
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 33-84 7.64e-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: 7.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1844083926  33 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 84
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-212 8.20e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  21 HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSLET----- 95
Cdd:COG4717   312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGVEDeeelr 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  96 -------QKLDLMTEVSELKLKLVGmEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQE 168
Cdd:COG4717   389 aaleqaeEYQELKEELEELEEQLEE-LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1844083926 169 QVAL--KDAEIERLHSQLSRTAalhseshterdQEIQRLKMGMETL 212
Cdd:COG4717   468 DGELaeLLQELEELKAELRELA-----------EEWAALKLALELL 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-230 8.56e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  32 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 108
Cdd:COG4717    71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 109 LKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLK-ATKAEVAQLQEQVALKDAEIERLHSQLSRT 187
Cdd:COG4717   139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEA 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1844083926 188 aalhSESHTERDQEIQRLKMGMETlllanEDKDRRIEELTGLL 230
Cdd:COG4717   219 ----QEELEELEEELEQLENELEA-----AALEERLKEARLLL 252
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 23-238 1.21e-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: 42.19  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  23 SAASNETYQER--LARLEGDKESLILQvsvLTDQVEAQGEKIRDLEVCLEghQVKlNAAEEMLQQellsRTSLETQKLDL 100
Cdd:pfam07888 107 SASSEELSEEKdaLLAQRAAHEARIRE---LEEDIKTLTQRVLERETELE--RMK-ERAKKAGAQ----RKEEEAERKQL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 101 MTEVSELKLKLVGMEKEQREQEEKQRKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERL 180
Cdd:pfam07888 177 QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGL 256

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926 181 HSQLSRTAALHSESHTERDQeiQRLKMGMETLLLAN------EDKDRRIEELTGLLNQYRKVKE 238
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQLADaslalrEGRARWAQERETLQQSAEADKD 318
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-257 1.92e-03

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: 41.98  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   28 ETYQERLARLE--------GDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQEllsrtsleTQKLD 99
Cdd:TIGR02169  211 ERYQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--------NKKIK 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  100 LMTEVSELKLKlvgmekeqreqeekqRKAEELLQELRHLKIKVEELENERNQYEwklkatkAEVAQLQEQVALKDAEIER 179
Cdd:TIGR02169  283 DLGEEEQLRVK---------------EKIGELEAEIASLERSIAEKERELEDAE-------ERLAKLEAEIDKLLAEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  180 LHSQLSRTAAlhseshtERDQ---EIQRLKMGMETLLLANEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERTLSINEE 256
Cdd:TIGR02169  341 LEREIEEERK-------RRDKlteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413


                   .
gi 1844083926  257 E 257
Cdd:TIGR02169  414 E 414
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 569-622 2.39e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.31  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1844083926 569 VTRWL-DDIGLPQYKDQFHESRVDRRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 622
Cdd:cd09504    10 TVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 486-537 2.45e-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: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1844083926 486 NAPFAQWSTERVCAWLEDFGLAQYV-IFARQWVsSGHTLLTATPQDMeKELGI 537
Cdd:cd09512     1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 43-232 2.47e-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: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  43 SLILQVSVLTDQVEAqgeKIRDLEVCLEGHQVKLNAAEEMLQQEllsrtsletqkldlMTEVSELKLKLVGMEKEQREQE 122
Cdd:pfam15905 156 SLSMELMKLRNKLEA---KMKEVMAKQEGMEGKLQVTQKNLEHS--------------KGKVAQLEEKLVSTEKEKIEEK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 123 EKQrkaEELLQElrhlkikVEELENERNQYEwklkATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTERDQEI 202
Cdd:pfam15905 219 SET---EKLLEY-------ITELSCVSEQVE----KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC 284

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1844083926 203 QRLKMGMETLLLANEDKDRR----IEELTGLLNQ 232
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTlnaeLEELKEKLTL 318
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-238 2.92e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELklk 110
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL--- 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  111 lvgmekeqreqeekqrkaEELLQELRHlkikveelenERNQYEWKLKATKAEVAQLQEQVAlkdaeierlhSQLSRTAAL 190
Cdd:TIGR02168  914 ------------------RRELEELRE----------KLAQLELRLEGLEVRIDNLQERLS----------EEYSLTLEE 955

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083926  191 HSESHTERDQEIQRLKmgmetlllanedkdRRIEELTGLLNQ-----------YRKVKE 238
Cdd:TIGR02168  956 AEALENKIEDDEEEAR--------------RRLKRLENKIKElgpvnlaaieeYEELKE 1000
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 14-234 2.93e-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: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   14 LKRSQVNHHSAASNETYQERLARLEGDKESLILQV--------SVLTDQVEAQGEKIRDLEVCLEGHQVK-LNAAEEMLQ 84
Cdd:TIGR00618  621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrehALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLA 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926   85 QELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQREQEEKQRKAEELLQELRHL---KIKVEELENER-NQYEWKLKATK 160
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENAS---SSLGSDLAAREDALNQSLKELMHQartVLKARTEAHFNnNEEVTAALQTG 777

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083926  161 AEVAQLQEQVALKDAEIERLHSQLsrtAALHSESHTERDQEIQRLKMGMETLLLANEDKDRRIEELTGLLNQYR 234
Cdd:TIGR00618  778 AELSHLAAEIQFFNRLREEDTHLL---KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-232 3.15e-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: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  133 QELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTaalhSESHTERDQEIQRLKMGMETL 212
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQL 752

                           90       100
                   ....*....|....*....|
gi 1844083926  213 LLANEDKDRRIEELTGLLNQ 232
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEE 772
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-235 3.93e-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: 40.52  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 129 EELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRT----AALHSESHTERDQEIQR 204
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAELEAQKEELAEL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1844083926 205 L----KMGME---TLLLANEDKDR--RIEELTGLLNQYRK 235
Cdd:COG4942   110 LralyRLGRQpplALLLSPEDFLDavRRLQYLKYLAPARR 149
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-239 4.02e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  53 DQVEAQGEKIRDLEvcleghqvklnAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqreqeekqrkaeELL 132
Cdd:COG4717    71 KELKELEEELKEAE-----------EKEEEYAELQEELEELEEELEELEAELEELREELEKL---------------EKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 133 QELRHLKIKVEELENERNQYEWK---LKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHTER----DQEIQRL 205
Cdd:COG4717   125 LQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEEL 204

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1844083926 206 KMGMETLLLANEDKDRRIEELTGLLNQYRKVKEI 239
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEA 238
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
129-278 4.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 129 EELLQELRHLKIKVEELENErnqyewKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALHSESHT---------ERD 199
Cdd:PRK03918  499 KELAEQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekkldeleEEL 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 200 QEIQR--LKMGMETLllanEDKDRRIEELTGLLNQYRKVKEIVMVTQGPSERtLSINEEEPEGGFSKWNATNKDPEELFK 277
Cdd:PRK03918  573 AELLKelEELGFESV----EELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRK 647


                  .
gi 1844083926 278 Q 278
Cdd:PRK03918  648 E 648
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 33-238 4.35e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  33 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlMTEVSELKlklv 112
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNK---- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 113 gmekeqreqeekqrKAEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAAlhs 192
Cdd:COG1579    90 --------------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA--- 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 193 eshtERDQEIQRLKmgmetlllanedkdRRIEELTG-----LLNQYRKVKE 238
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 ...
 490-538 4.96e-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: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 490 AQWSTERVCAWLE--DFGLAQYVIFARQWVSSGHTLLTATPQDMEkELGIK 538
Cdd:cd09511     2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 31-170 7.14e-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: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  31 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 94
Cdd:COG1579    30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926  95 TQKLDLMTEVSELKLKLvgmekeqreqeekqRKAEELLQELR-HLKIKVEELENERNQYEWKLKATKAEVAQLQEQV 170
Cdd:COG1579   110 DEILELMERIEELEEEL--------------AELEAELAELEaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 500-554 8.18e-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: 35.73  E-value: 8.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844083926 500 WLEDFGLAQYV-IFARQWVSSGHTLLTATPQDMEkELGIKHPLHRKKLVLAVKAIN 554
Cdd:cd09498    13 WLSLLGLPQYHkVLVENGYDSIDFVTDLTWEDLQ-DIGITKLGHQKKLMLAIKKLK 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
128-239 8.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926 128 AEELLQELRHLKIKVEELENERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQLSRTAALH---------SESHTER 198
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklSEFYEEY 305

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1844083926 199 DQEIQRLKMGMETL--LLAN--------EDKDRRIEELTGLLNQYRKVKEI 239
Cdd:PRK03918  306 LDELREIEKRLSRLeeEINGieerikelEEKEERLEELKKKLKELEKRLEE 356
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 128-184 8.61e-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: 8.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083926 128 AEELLQELRHLKIKVEElenERNQYEWKLKATKAEVAQLQEQVALKDAEIERLHSQL 184
Cdd:pfam20492  60 AEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 17-251 9.15e-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: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  17 SQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRTSLETQ 96
Cdd:pfam05557  58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083926  97 KLDLMTEVSELKLKLVGMEKEQREQeekqrkaEELLQELRHLKIKVEELENERNQYE-WK--LKATKAEVAQLQEQvalk 173
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDSeiVKNSKSELARIPEL---- 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083926 174 DAEIERLHSqlsrtaalhseshterdqEIQRLKMGMETLLLANEDKdrriEELTGLLNQYRKVKEIVMVTQGPSERTL 251
Cdd:pfam05557 203 EKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLKRKLEREEKYREEAATLELEKEKLE 258
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 492-537 9.54e-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: 9.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1844083926 492 WSTERVCAWLEDFGLAQYVI--FARQWVsSGHTLLTATPQDMeKELGI 537
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSVCekFRENEI-TGDILLELDLEDL-KELDI 48
 
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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