NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568949847|ref|XP_006507513|]
View 

liprin-beta-2 isoform X7 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 570-641 7.04e-45

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.92  E-value: 7.04e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 570 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 641
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 ...
 485-547 2.17e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.17e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 485 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 547
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 ...
 411-474 2.64e-36

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


:

Pssm-ID: 188962  Cd Length: 64  Bit Score: 130.43  E-value: 2.64e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847 411 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 474
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
56-167 1.48e-06

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


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.78  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  56 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 135
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568949847 136 ETLLVANEDKDRRIEELTGLLNKYLRVKEIVM 167
Cdd:COG2433  475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
CBD_TRPV5_C super family cl41698
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 269-314 5.41e-03

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


The actual alignment was detected with superfamily member cd22296:

Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949847 269 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 314
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 570-641 7.04e-45

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.92  E-value: 7.04e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 570 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 641
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 ...
 485-547 2.17e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.17e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 485 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 547
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 ...
 411-474 2.64e-36

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 130.43  E-value: 2.64e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847 411 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 474
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 490-546 6.18e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 6.18e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847  490 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 413-475 5.18e-16

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 72.69  E-value: 5.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  413 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 475
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 411-475 8.61e-13

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.85  E-value: 8.61e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949847   411 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 475
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
571-641 3.56e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.90  E-value: 3.56e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847  571 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 641
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 491-546 6.92e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.68  E-value: 6.92e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847   491 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 571-640 2.49e-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: 51.14  E-value: 2.49e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   571 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 640
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
56-167 1.48e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.78  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  56 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 135
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568949847 136 ETLLVANEDKDRRIEELTGLLNKYLRVKEIVM 167
Cdd:COG2433  475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 16-152 2.78e-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: 50.83  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    16 SRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQ----ELKHLKIKVEELENERNQYEWELKATKAEVA 91
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847    92 QLQEQValkDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 152
Cdd:TIGR02168  786 ELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 59-181 3.52e-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: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    59 LQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----------RSA-ALHSDHAERDQE 127
Cdd:pfam15921  530 LQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgRTAgAMQVEKAQLEKE 598

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568949847   128 IHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 181
Cdd:pfam15921  599 INDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-204 6.82e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  21 ETQKLDLMtevSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIK-------------VEELENERNQYEWE-LKAT 86
Cdd:PRK03918 447 EEHRKELL---EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliklkelaeqLKELEEKLKKYNLEeLEKK 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  87 KAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNK 158
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNE 603

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568949847 159 YLRVKEIVMATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 204
Cdd:PRK03918 604 YLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 269-314 5.41e-03

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


Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949847 269 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 314
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 570-641 7.04e-45

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.92  E-value: 7.04e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 570 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 641
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 ...
 485-547 2.17e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 136.29  E-value: 2.17e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 485 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 547
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 ...
 411-474 2.64e-36

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


Pssm-ID: 188962  Cd Length: 64  Bit Score: 130.43  E-value: 2.64e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847 411 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 474
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 ...
 578-639 8.32e-30

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 111.86  E-value: 8.32e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 578 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 639
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 ...
 570-641 2.17e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 111.00  E-value: 2.17e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 570 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 641
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 ...
 489-547 1.28e-28

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 108.39  E-value: 1.28e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847 489 IWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 547
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 ...
 418-474 1.57e-27

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


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.39  E-value: 1.57e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949847 418 RVCTWMEDFGLGQ-YVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 474
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 ...
 570-641 3.83e-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: 84.68  E-value: 3.83e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 570 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 641
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 490-546 6.18e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 6.18e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847  490 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 413-475 5.18e-16

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 72.69  E-value: 5.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  413 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 475
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 485-547 2.37e-15

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 70.90  E-value: 2.37e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949847 485 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 547
Cdd:cd09567    1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 411-475 8.61e-13

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.85  E-value: 8.61e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949847   411 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 475
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 490-543 1.40e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 62.64  E-value: 1.40e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568949847 490 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 543
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
571-641 3.56e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.90  E-value: 3.56e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847  571 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 641
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 418-473 4.22e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 61.49  E-value: 4.22e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949847 418 RVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 473
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
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 ...
 486-546 7.30e-10

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 55.56  E-value: 7.30e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 486 LDHIWV-TRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 546
Cdd:cd09565    1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 491-546 6.92e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.68  E-value: 6.92e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847   491 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 571-640 2.49e-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: 51.14  E-value: 2.49e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   571 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 640
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
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 ...
 411-475 1.48e-07

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


Pssm-ID: 188961  Cd Length: 71  Bit Score: 49.10  E-value: 1.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847 411 FAQWSTERVCTWMEDF-GL-GQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 475
Cdd:cd09562    1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 412-472 5.10e-07

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


Pssm-ID: 188963  Cd Length: 70  Bit Score: 47.45  E-value: 5.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 412 AQWSTERVCTWME-DFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 472
Cdd:cd09564    2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
414-475 1.34e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  414 WSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 475
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
56-167 1.48e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.78  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  56 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 135
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568949847 136 ETLLVANEDKDRRIEELTGLLNKYLRVKEIVM 167
Cdd:COG2433  475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 16-152 2.78e-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: 50.83  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    16 SRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQ----ELKHLKIKVEELENERNQYEWELKATKAEVA 91
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847    92 QLQEQValkDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 152
Cdd:TIGR02168  786 ELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
491-543 4.79e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.57  E-value: 4.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568949847  491 VTRWLDDIGLPQYKDQFHESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 543
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 410-473 5.35e-06

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 44.33  E-value: 5.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568949847 410 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 473
Cdd:cd09507    1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 491-544 7.30e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 43.84  E-value: 7.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568949847 491 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 544
Cdd:cd09533    2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 414-475 9.17e-06

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 43.85  E-value: 9.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 414 WSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 475
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 414-470 1.03e-05

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 43.86  E-value: 1.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847 414 WSTERVCTWMEDF-GLGQYVIFARQWVTSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 470
Cdd:cd09504    5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 56-158 1.20e-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: 48.90  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    56 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA----LHSDHAERDQEIHR- 130
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrrerLQQEIEELLKKLEEa 433

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568949847   131 -----------LKMGMETLLVANEDKDRRIEELTGLLNK 158
Cdd:TIGR02168  434 elkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 488-546 1.27e-05

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 43.46  E-value: 1.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 488 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:cd09506    3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 491-546 1.68e-05

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 43.08  E-value: 1.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949847 491 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:cd09530    8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-185 2.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLK 132
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568949847 133 mgMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGPSERTLSINEDEIE 185
Cdd:COG1196  375 --AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 59-181 3.52e-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: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    59 LQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----------RSA-ALHSDHAERDQE 127
Cdd:pfam15921  530 LQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgRTAgAMQVEKAQLEKE 598

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568949847   128 IHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 181
Cdd:pfam15921  599 INDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 488-544 5.80e-05

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 41.93  E-value: 5.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847 488 HIW----VTRWL-DDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 544
Cdd:cd09504    3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 412-473 6.01e-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: 41.47  E-value: 6.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847 412 AQWSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 473
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-204 6.82e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  21 ETQKLDLMtevSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIK-------------VEELENERNQYEWE-LKAT 86
Cdd:PRK03918 447 EEHRKELL---EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliklkelaeqLKELEEKLKKYNLEeLEKK 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  87 KAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNK 158
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNE 603

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568949847 159 YLRVKEIVMATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 204
Cdd:PRK03918 604 YLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 54-116 8.15e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 8.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  54 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA 116
Cdd:COG3883   31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
28-164 1.21e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  28 MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA--TKAEVAQLQEQVALKDAEIE 105
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLE 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568949847 106 RLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLvaNEDKDRRIEELTGLLNKYLRVKE 164
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELL--EQLSLATEEELQDLAEELEELQQ 206
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 419-472 1.55e-04

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 40.47  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568949847 419 VC-TWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 472
Cdd:cd09567    7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 415-468 1.93e-04

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 39.93  E-value: 1.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847 415 STERVCTWMEDFGLGQYvifARQWVTSGHTLLT---ATPQDMeKELGIKHPLHRKKL 468
Cdd:cd09497    3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-163 3.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQY--EWELKATKAEVAQLQEQVALKDAEIERLHSQLsrsaalhsdhAERDQEIHR 130
Cdd:COG4717  395 EEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELREEL----------AELEAELEQ 464

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568949847 131 LKMGmETLLVANEDKDRRIEELTGLLNKYLRVK 163
Cdd:COG4717  465 LEED-GELAELLQELEELKAELRELAEEWAALK 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-170 3.73e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHrlk 132
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE--- 322

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568949847 133 mgmETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQ 170
Cdd:COG1196  323 ---EELAELEEELEELEEELEELEEELEEAEEELEEAE 357
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-164 7.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQY---EWELKATKAEVAQLQEQVALKDAEIERLHSQLsrsaalhsDHAERDQEIH 129
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLL--------QLLPLYQELE 135

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568949847 130 RLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKE 164
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELEELEA 170
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 17-236 7.51e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    17 RTSLETQKLDLMTEVSELKLKlvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEwelKATKAEVAQLQEQ 96
Cdd:pfam02463  302 LLKLERRKVDDEEKLKESEKE---KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEEL 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    97 VALKDAEIERLHSQLSRSAALHS----DHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGP 172
Cdd:pfam02463  376 LAKKKLESERLSSAAKLKEEELElkseEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847   173 SERTLSINEDEIEGSFRKWNTTNKSPEEVPKQEispRCSSPTPGPPPLPQKSLESRAQKKLSCS 236
Cdd:pfam02463  456 QELKLLKDELELKKSEDLLKETQLVKLQEQLEL---LLSRQKLEERSQKESKARSGLKVLLALI 516
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
56-113 7.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 7.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568949847  56 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR 113
Cdd:COG4372  104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 21-186 7.92e-04

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: 42.05  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   21 ETQKLdlMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQE-LKHLKIKVEELENERNQYEWELKATKAEV----AQLQE 95
Cdd:pfam09787  62 EIQKL--RGQIQQLRTELQELEAQQQEEAESSREQLQELEEqLATERSARREAEAELERLQEELRYLEEELrrskATLQS 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   96 QVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLkmgMETLLvaneDKDRRIEELT----GLLNKYLRVKEIVMATQG 171
Cdd:pfam09787 140 RIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL---TETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQG 212

                         170
                  ....*....|....*
gi 568949847  172 PSERTLSINEDEIEG 186
Cdd:pfam09787 213 EGSNGTSINMEGISD 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
53-204 7.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS-------------AALHS 119
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekaeeyiklSEFYE 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847 120 DHAERDQEIHRLK-------MGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGPSERTLSInEDEIEGsfRKWN 192
Cdd:PRK03918 304 EYLDELREIEKRLsrleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELER--LKKR 380

                        170
                 ....*....|..
gi 568949847 193 TTNKSPEEVPKQ 204
Cdd:PRK03918 381 LTGLTPEKLEKE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-159 8.51e-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: 42.75  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    16 SRTSLETQKLD---LMTEVSELKLKlvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQ 92
Cdd:TIGR02169  341 LEREIEEERKRrdkLTEEYAELKEE---LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847    93 LQEQVALKDAEIERLHSQLsrsAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKY 159
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKI---NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 412-460 1.05e-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: 38.04  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568949847 412 AQWSTERVCTWME--DFGLGQYVIFARQWVTSGHTLLTATPQDMEkELGIK 460
Cdd:cd09511    2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 26-168 1.06e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.50  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   26 DLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQElKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIE 105
Cdd:pfam10174 615 EQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD-NSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLT 693

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  106 RLHsqlsrsaalhsdHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMA 168
Cdd:pfam10174 694 NLR------------AERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMA 744
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 53-111 1.16e-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: 39.52  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568949847   53 RKAEELLQELKHLKIKVEElenERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 111
Cdd:pfam20492  58 QEAEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-161 1.37e-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: 42.35  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    54 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKM 133
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100
                   ....*....|....*....|....*...
gi 568949847   134 GMETLLVANEDKdrrIEELTGLLNKYLR 161
Cdd:TIGR02168  772 EAEEELAEAEAE---IEELEAQIEQLKE 796
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 491-525 1.58e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 37.61  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 568949847 491 VTRWLDDIGLPQYKDQF-HESRVDGRMLQYLTVNDL 525
Cdd:cd09515    9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 53-114 1.63e-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: 40.68  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS 114
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-211 2.10e-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: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    23 QKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHlkiKVEELENERNQYEWELKATKAEVAQLQEQVALKDA 102
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   103 EIERLHSQLSRSAA-------------------------LHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLN 157
Cdd:TIGR02168  310 RLANLERQLEELEAqleeleskldelaeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568949847   158 KYLRVKEIVMATQGPSERTLSINEDEIEGSFRKWNTTNKSPEEVPKQEISPRCS 211
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
54-158 3.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  54 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQvaLKDAEiERLHSQLSRSAALHSDHAERDQEIHRLKM 133
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE--LEELN-EQLQAAQAELAQAQEELESLQEEAEELQE 115

                         90       100
                 ....*....|....*....|....*
gi 568949847 134 GMETLLVANEDKDRRIEELTGLLNK 158
Cdd:COG4372  116 ELEELQKERQDLEQQRKQLEAQIAE 140
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 53-113 4.19e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 4.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR 113
Cdd:COG4942   48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 488-546 4.22e-03

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.47  E-value: 4.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847 488 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 546
Cdd:cd09575    3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_STIM2 cd09574
SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal ...
 488-535 4.26e-03

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


Pssm-ID: 188973  Cd Length: 74  Bit Score: 36.50  E-value: 4.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847 488 HIWVT----RWLDD-IGLPQYKDQFHESRVDGRMLQYLTVNDLLF----LKVTSQLH 535
Cdd:cd09574    3 HNWTMedtlQWLKEfVELPQYEKNFRDNNVKGTTLPRIAVNEPSFmisqLKILDRSH 59
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-165 4.86e-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: 40.44  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847    53 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRsaalhsdhaERDQEIHRLK 132
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAEL 800

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568949847   133 MGMETLLVANEdkdRRIEELTGLLNKYLRVKEI 165
Cdd:TIGR02169  801 SKLEEEVSRIE---ARLREIEQKLNRLTLEKEY 830
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-152 5.27e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  54 KAEELLQELKHLKIKVEELENERNQyewELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKM 133
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                         90
                 ....*....|....*....
gi 568949847 134 GMETLLVANEDKDRRIEEL 152
Cdd:COG1196  415 RLERLEEELEELEEALAEL 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
53-132 5.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   53 RKAEELLQELKHLKIKVEELENERNQYE-------WELKATKAEVAQLQEQVA--------LKDAEIERLHSQLSRSAAL 117
Cdd:COG4913   338 DRLEQLEREIERLERELEERERRRARLEallaalgLPLPASAEEFAALRAEAAallealeeELEALEEALAEAEAALRDL 417

                          90
                  ....*....|....*
gi 568949847  118 HSDHAERDQEIHRLK 132
Cdd:COG4913   418 RRELRELEAEIASLE 432
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 491-525 5.40e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 5.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568949847 491 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL 525
Cdd:cd09501    9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDEL 43
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 269-314 5.41e-03

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


Pssm-ID: 412091  Cd Length: 73  Bit Score: 36.19  E-value: 5.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568949847 269 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 314
Cdd:cd22296   12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 414-468 5.67e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 5.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949847 414 WSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMEKELGIKHPLHRKKL 468
Cdd:cd09501    4 WSVADVQTWLKQIGFEDYAeKFSESQV-DGDLLLQLTEDELKQDLGMSSGLLRKRF 58
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 410-475 5.72e-03

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.08  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568949847 410 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 475
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 414-459 5.80e-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: 35.99  E-value: 5.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568949847 414 WSTERVCTWMEDFGLGQYVI--FARQWVTsGHTLLTATPQDMeKELGI 459
Cdd:cd09535    3 WSPEQVAEWLLSAGFDDSVCekFRENEIT-GDILLELDLEDL-KELDI 48
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 408-459 6.01e-03

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 36.09  E-value: 6.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568949847 408 NAPFAQWSTERVCTWMEDFGLGQYV-IFARQWVTsGHTLLTATPQDMeKELGI 459
Cdd:cd09512    1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNID-GQQLLQLDSSKL-KALGI 51
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
56-138 7.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  56 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR----SAALHSDHAERDQEIHRL 131
Cdd:COG4372   76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleaqIAELQSEIAEREEELKEL 155


                 ....*..
gi 568949847 132 KMGMETL 138
Cdd:COG4372  156 EEQLESL 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-185 7.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  53 RKAEELLQELKHLKIKVEELENERNQYEWELKA-------TKAEVAQLQEQVALKDAEIERLHSQLSRSAA----LHSDH 121
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEEelaeLEEEL 332

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568949847 122 AERDQEIHRLKmgmETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQgpsERTLSINEDEIE 185
Cdd:COG1196  333 EELEEELEELE---EELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLE 390
PRK09039 PRK09039
peptidoglycan -binding protein;
19-164 7.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847  19 SLETQ-KLDLMTEVSELKLKLvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQL---- 93
Cdd:PRK09039  70 SLERQgNQDLQDSVANLRASL--------------SAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVsara 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949847  94 QEQVALKDAEIERLHSQLSRSAALHSDHAERDQEihrlkmgmetllvanedKDRRIEELTGLLNKYL--RVKE 164
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAALDASEKRDRE-----------------SQAKIADLGRRLNVALaqRVQE 191
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 56-141 7.78e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 38.02  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949847   56 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRsaaLHSDHAERDQEIHRLKMGM 135
Cdd:pfam05266 105 TKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIAR---LKSEAEKLEQEIQDVELEF 181


                  ....*.
gi 568949847  136 ETLLVA 141
Cdd:pfam05266 182 EATASA 187
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH