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Conserved domains on  [gi|1720421324|ref|XP_030098095|]
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liprin-beta-2 isoform X10 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 756-827 1.86e-44

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.86e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 756 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 827
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 ...
 671-733 3.38e-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: 3.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 671 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 733
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 ...
 597-660 3.27e-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: 130.81  E-value: 3.27e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 597 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 660
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-344 3.02e-11

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  141 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 213
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  214 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 293
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324  294 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 344
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
CBD_TRPV5_C super family cl41698
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 455-500 5.88e-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: 36.58  E-value: 5.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720421324 455 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 500
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 ...
 756-827 1.86e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.86e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 756 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 827
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 ...
 671-733 3.38e-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: 3.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 671 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 733
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 ...
 597-660 3.27e-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: 130.81  E-value: 3.27e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 597 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 660
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 676-732 8.06e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 8.06e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 676 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 599-661 6.89e-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: 6.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 599 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 661
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 597-661 1.51e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.47  E-value: 1.51e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324  597 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 661
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
757-827 5.83e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 5.83e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421324 757 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 827
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-344 3.02e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  141 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 213
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  214 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 293
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324  294 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 344
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 677-732 1.14e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.30  E-value: 1.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324  677 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 144-367 2.45e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.21  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 223
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 298
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324  299 -----RSA-ALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 367
Cdd:pfam15921  578 vgqhgRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 757-826 4.21e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.76  E-value: 4.21e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  757 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 826
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-317 8.13e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.54  E-value: 8.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 108 ALLSQVPGPTATYIKEWFEDSLSQVNHHGAASnetyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV 187
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 188 KLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKL---------VGMEKEQKEQEEKQRKAEELLQELK 249
Cdd:COG4942    84 ELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLLspedfldavRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 250 HLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS----RSAALHSDHAERDQEIHRL 317
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaaELAELQQEAEELEALIARL 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-390 9.39e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDK-ESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ------------------ELL 201
Cdd:PRK03918  375 ERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkELL 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 202 SRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVAQLQ 280
Cdd:PRK03918  455 EEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYEKLK 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 281 EQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNKYLRVKEIV 352
Cdd:PRK03918  532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLELKDAE 611

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720421324 353 MATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 390
Cdd:PRK03918  612 KELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 455-500 5.88e-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: 36.58  E-value: 5.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720421324 455 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 500
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 ...
 756-827 1.86e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.86e-44
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 756 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 827
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 ...
 671-733 3.38e-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: 3.38e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 671 LLDHIWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 733
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 ...
 597-660 3.27e-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: 130.81  E-value: 3.27e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 597 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 660
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 ...
 764-825 1.22e-29

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 111.86  E-value: 1.22e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 764 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 825
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 ...
 756-827 2.59e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 111.38  E-value: 2.59e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 756 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 827
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 ...
 675-733 1.53e-28

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 108.78  E-value: 1.53e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 675 IWVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 733
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 ...
 604-660 2.17e-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: 2.17e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324 604 RVCTWMEDFGLGQ-YVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 660
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 ...
 756-827 6.26e-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: 6.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 756 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 827
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 676-732 8.06e-17

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 75.38  E-value: 8.06e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 676 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 599-661 6.89e-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: 6.89e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 599 QWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 661
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 ...
 671-733 2.80e-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: 2.80e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324 671 LLDHIWVTR-WLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 733
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 597-661 1.51e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 63.47  E-value: 1.51e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324  597 FAQWSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 661
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 676-729 2.47e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 62.26  E-value: 2.47e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 676 WVTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 729
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
757-827 5.83e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 5.83e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421324 757 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 827
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 604-659 8.05e-12

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 61.10  E-value: 8.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421324 604 RVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 659
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-344 3.02e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.77  E-value: 3.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  141 ETYQERLARLEGDKESLILQVSVLTDQV-EAQGE------KIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDL 213
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIeELQKElyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  214 MTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERL 293
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324  294 HSQLSRSAA----LHSDHAERDQEIHR------------LKMGMETLLVANEDKDRRIEELTGLLNK 344
Cdd:TIGR02168  406 EARLERLEDrrerLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEELERLEEALEELREELEE 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-338 7.43e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.15  E-value: 7.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  164 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEE 243
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  244 LLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQValkDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMET 323
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170
                   ....*....|....*
gi 1720421324  324 LLVANEDKDRRIEEL 338
Cdd:TIGR02168  829 LERRIAATERRLEDL 843
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 ...
 672-732 7.84e-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: 7.84e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 672 LDHIWV-TRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 732
Cdd:cd09565     1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 677-732 1.14e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 52.30  E-value: 1.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324  677 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 144-367 2.45e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.21  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 223
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLS----- 298
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324  299 -----RSA-ALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKyLRVKEIVMATQGpSERTLSINE 367
Cdd:pfam15921  578 vgqhgRTAgAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKD 650
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-345 2.69e-08

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: 58.16  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   89 LIEDLRLALEmlalpqEREALLSQVpgptATYIKEWFEDSLSQVnhhgaasnetyQERLARLEGDKESLILQVSVLTDQV 168
Cdd:TIGR02169  259 EISELEKRLE------EIEQLLEEL----NKKIKDLGEEEQLRV-----------KEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  169 EAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQEL 248
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----------EEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  249 KHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLsrsAALHSDHAERDQEIHRLKMGMETLLVAN 328
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI---NELEEEKEDKALEIKKQEWKLEQLAADL 464

                          250
                   ....*....|....*..
gi 1720421324  329 EDKDRRIEELTGLLNKY 345
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRV 481
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 757-826 4.21e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.76  E-value: 4.21e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  757 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 826
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-317 8.13e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.54  E-value: 8.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 108 ALLSQVPGPTATYIKEWFEDSLSQVNHHGAASnetyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV 187
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 188 KLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKL---------VGMEKEQKEQEEKQRKAEELLQELK 249
Cdd:COG4942    84 ELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLLspedfldavRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 250 HLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS----RSAALHSDHAERDQEIHRL 317
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaaELAELQQEAEELEALIARL 232
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 ...
 597-661 1.96e-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: 1.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 597 FAQWSTERVCTWMEDF-GL-GQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 661
Cdd:cd09562     1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
86-296 4.45e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 4.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   86 VLHLIEDLRLALEMLALPQEREALLSQVPGPTATYIKEW-----FEDSLSQVNHHGAA-SNETYQERLARLEGDKESLIL 159
Cdd:COG4913    230 LVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARerlaeLEYLRAALRLWFAQrRLELLEAELEELRAELARLEA 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  160 QVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqkeqeekq 238
Cdd:COG4913    310 ELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS----------- 378

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324  239 rkAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 296
Cdd:COG4913    379 --AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-350 5.74e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEG-------HQVKLNAAEEMLQQELLSRTSLETQKLDL 213
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarLEERRRELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 214 MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKI-KVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 292
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324 293 LHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKE 350
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 598-658 6.75e-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: 6.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 598 AQWSTERVCTWME-DFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 658
Cdd:cd09564     2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 144-343 6.92e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 223
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 224 LvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA-TKAEVAQLQEQVALKDAEIERLHSQLSRSAA 302
Cdd:COG1196   388 L----------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720421324 303 LHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLN 343
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-390 9.39e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDK-ESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ------------------ELL 201
Cdd:PRK03918  375 ERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkELL 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 202 SRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVAQLQ 280
Cdd:PRK03918  455 EEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYEKLK 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 281 EQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLL--------VANEDKDRRIEELTGLLNKYLRVKEIV 352
Cdd:PRK03918  532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfESVEELEERLKELEPFYNEYLELKDAE 611

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720421324 353 MATQGPSERtLSINEDEIEGSFRKWNTTNKSPEEVPKQ 390
Cdd:PRK03918  612 KELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKE 648
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
242-353 1.60e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 52.17  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 242 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 321
Cdd:COG2433   409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720421324 322 ETLLVANEDKDRRIEELTGLLNKYLRVKEIVM 353
Cdd:COG2433   475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
600-661 2.11e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 600 WSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 661
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 142-338 2.52e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 142 TYQERLARLegDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELK 221
Cdd:COG1196   217 ELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 222 LKLVGMEKEQKEQEEKQR----KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 297
Cdd:COG1196   295 AELARLEQDIARLEERRReleeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720421324 298 ----SRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 338
Cdd:COG1196   375 aeaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-322 2.91e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   90 IEDLRLALEMLalpQEREALLSQVPGPTATYIKEwfedsLSQVNHHGAASNETYQERLARLEGDKESLILQVSVLTD--- 166
Cdd:TIGR02169  718 IGEIEKEIEQL---EQEEEKLKERLEELEEDLSS-----LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArls 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  167 -----QVEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVgmeKEQKEQEEKQRKA 241
Cdd:TIGR02169  790 hsripEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNGKK 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  242 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGM 321
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943


                   .
gi 1720421324  322 E 322
Cdd:TIGR02169  944 E 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-338 3.37e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 223
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 LVGMEKEQKEQEEKQRKAEELLQ-----------ELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 292
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720421324  293 LHSQLSRS----AALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEEL 338
Cdd:TIGR02168  857 LAAEIEELeeliEELESELEALLNERASLEEALALLRSELEELSEELREL 906
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 145-422 3.83e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.13  E-value: 3.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  145 ERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ-VKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 223
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 lvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEwelKATKAEVAQLQEQVALKDAEIERLHSQLSRSAAL 303
Cdd:pfam02463  323 ---KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  304 HS----DHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGPSERTLSINEDEIEGSFRKWNT 379
Cdd:pfam02463  397 LElkseEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1720421324  380 TNKSPEEVPKQEispRCSSPTPGPPPLPQKSLESRAQKKLSCS 422
Cdd:pfam02463  477 TQLVKLQEQLEL---LLSRQKLEERSQKESKARSGLKVLLALI 516
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 140-339 4.20e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 140 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 214
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 215 TEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKAtkaevaqlqeqvalKDAEIERLH 294
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD--------------LEDELNKDD 551

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720421324 295 SQLSRSaALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELT 339
Cdd:TIGR04523 552 FELKKE-NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 596-659 5.26e-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: 44.71  E-value: 5.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324 596 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 659
Cdd:cd09507     1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 143-372 5.50e-06

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 49.37  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 143 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRTslETQKLdlMTEVSELKL 222
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLRE--EIQKL--RGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 223 KLVGMEKEQKEQEEKQRKAEELLQE-LKHLKIKVEELENERNQYEWELKATKAEV----AQLQEQVALKDAEIERLHSQL 297
Cdd:pfam09787  76 ELQELEAQQQEEAESSREQLQELEEqLATERSARREAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRNQL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421324 298 SRSAALHSDHAERDQEIHRLkmgMETLLvaneDKDRRIEELT----GLLNKYLRVKEIVMATQGPSERTLSINEDEIEG 372
Cdd:pfam09787 156 TSKSQSSSSQSELENRLHQL---TETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGISD 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
144-296 6.34e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVS 218
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324 219 ELKLKLVgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 296
Cdd:COG4717   174 ELQEELE---------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
677-729 7.11e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.57  E-value: 7.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 677 VTRWLDDIGLPQYKDQFHESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 729
Cdd:pfam07647   9 VADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 677-730 1.12e-05

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 43.46  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 677 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 730
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 600-656 1.15e-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: 44.25  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421324 600 WSTERVCTWMEDF-GLGQYVIFARQWVTSGHTL---LTATPQDMEKELGIKHPLHRKKLVL 656
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 600-661 1.33e-05

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 43.85  E-value: 1.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 600 WSTERVCTWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 661
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 674-732 1.37e-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: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 674 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:cd09506     3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 105-352 1.97e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  105 EREALLSQVPGPTATY--IKEWFEDSLSQVNHHGAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLE 179
Cdd:pfam15921  549 ECEALKLQMAEKDKVIeiLRQQIENMTQLVGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELE 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  180 VC---LEGHQVKL-NAAEEMLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQkeqeekqrkaeELLQelKHLKIKV 255
Cdd:pfam15921  625 ARvsdLELEKVKLvNAGSERLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKS 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  256 EELENERNQYEWELKATKAEVAQ---------------------LQEQVALKDAEIERLHSQLSrsaALHSDHAERDQEI 314
Cdd:pfam15921  688 EEMETTTNKLKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQ---FLEEAMTNANKEK 764

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1720421324  315 HRL-----KMGMETLLVANEdKDRRIEELTGLLNKYLRVKEIV 352
Cdd:pfam15921  765 HFLkeeknKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKV 806
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 677-732 2.20e-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: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421324 677 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:cd09530     8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 141-340 2.78e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.18  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLarleGDKESlilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLSRtsLETQKLDLMTEVS 218
Cdd:pfam05483 229 EEYKKEI----NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 219 ELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLK-IKVEELENERNQYEW---ELKATKAEVAQL-----------QEQV 283
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAAHSFvvtEFEATTCSLEELlrteqqrleknEDQL 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 284 ALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTG 340
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-429 2.93e-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: 48.13  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLEVCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSELKLK 223
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 LvgmekeqkeqeekqRKAEELLQELKHlkiKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA- 302
Cdd:TIGR02168  262 L--------------QELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAq 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  303 ------------------------LHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGP 358
Cdd:TIGR02168  325 leeleskldelaeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421324  359 SERTLSINEDEIEGSFRKWNTTNKSPEEVPKQEISPRCSSPTPGPPPLPQKSLESRAQKKlscSLEDLRRE 429
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE---ELREELEE 472
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 141-302 3.05e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 198
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 199 ---ELLSRTS----LETQKLDLMTEVSELKLKLvgmekeQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA 271
Cdd:COG3883   113 sfsDFLDRLSalskIADADADLLEELKADKAEL------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720421324 272 TKAEVAQLQEQVALKDAEIERLHSQLSRSAA 302
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-299 5.41e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 137 AASNETYQERLARLEgdkeSLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellSRTSLETQKLDLMTE 216
Cdd:COG4372    27 AALSEQLRKALFELD----KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 217 VSELklklvgmekeqkeqeekqrkaEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 296
Cdd:COG4372   100 QEEL---------------------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158


                  ...
gi 1720421324 297 LSR 299
Cdd:COG4372   159 LES 161
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 674-730 5.78e-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: 42.32  E-value: 5.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 674 HIW----VTRWL-DDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 730
Cdd:cd09504     3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 598-659 7.49e-05

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 41.85  E-value: 7.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 598 AQWSTERVCTWMEDFGLGQYV-IFARQWVTSGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 659
Cdd:cd09515     2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-351 9.03e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 9.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  166 DQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqELLSRTSLETQKL-DLMTEVSELKlklvgmekeqkeqeekqRKAEEL 244
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIgEIEKEIEQLE-----------------QEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  245 LQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRsaalhsdhaERDQEIHRLKMGMETL 324
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEE 806

                          170       180
                   ....*....|....*....|....*..
gi 1720421324  325 LVANEdkdRRIEELTGLLNKYLRVKEI 351
Cdd:TIGR02169  807 VSRIE---ARLREIEQKLNRLTLEKEY 830
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 89-302 1.12e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   89 LIEDLRLALEMLalpQEREALLSQVPGPTATYIKEWFEDSLSQvnhhgAASNETYQERLARLEGDKESLILQVSVLTDQV 168
Cdd:TIGR02168  296 EISRLEQQKQIL---RERLANLERQLEELEAQLEELESKLDEL-----AEELAELEEKLEELKEELESLEAELEELEAEL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  169 EAQGEKIRDLEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQR 239
Cdd:TIGR02168  368 EELESRLEELEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324  240 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQV-ALKDaeIERLHSQLSRSAA 302
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdSLER--LQENLEGFSEGVK 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-339 1.67e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSEL 220
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 221 KLKLvgmekeqkeqeekqrkaEELLQELKHLKIKVEELENERNQyEW------ELKATKAEVAQLQEQVALKDAEIERLH 294
Cdd:TIGR04523 280 NKKI-----------------KELEKQLNQLKSEISDLNNQKEQ-DWnkelksELKNQEKKLEEIQNQISQNNKIISQLN 341

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720421324 295 SQLSR----SAALHSDHAERDQEIHRLKMGMETLLVANEDKDRRIEELT 339
Cdd:TIGR04523 342 EQISQlkkeLTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 605-658 1.86e-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: 1.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720421324 605 VC-TWMEDFGLGQYVIFARQWVTSGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 658
Cdd:cd09567     7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 240-302 2.57e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 240 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAA 302
Cdd:COG3883    31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 601-654 2.76e-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: 2.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 601 STERVCTWMEDFGLGQYvifARQWVTSGHTLLT---ATPQDMeKELGIKHPLHRKKL 654
Cdd:cd09497     3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-313 2.80e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 101 ALPQEREALLSQvpgptatyiKEWFEDSLSQVNHHGAASN---ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 177
Cdd:PRK02224  311 AVEARREELEDR---------DEELRDRLEECRVAAQAHNeeaESLREDADDLEERAEELREEAAELESELEEAREAVED 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 178 LEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELL---------QEL 248
Cdd:PRK02224  382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPV 461

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421324 249 KHLKI---------KVEELENERNQYEWELKATKAEVAQLQEQVALKDaEIERLHSQLSRSAALHSDHAERDQE 313
Cdd:PRK02224  462 EGSPHvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEE 534
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 121-354 4.18e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.04  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 121 IKEWFEDSLSQVNHHGAASNETYQERLarlegdKESLILQVSVLTDQV--------EAQGEKIRDLEVCLEGHQVKLNAA 192
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAVRT------NPEINDRIRLLEQEVarykeesgKAQAEVERLLGILREVENEKNDKD 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 193 EEMlqQELLSRTSLetQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQElKHLKIKVEELENERNQYEWELKAT 272
Cdd:pfam10174 600 KKI--AELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD-NSQQLQLEELMGALEKTRQELDAT 674

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 273 KAEVAQLQEQVALKDAEIERLHsqlsrsaalhsdHAERDQEIHRLKMGMETLLVANEDKDRRIEELTGLLNKYLRVKEIV 352
Cdd:pfam10174 675 KARLSSTQQSLAEKDGHLTNLR------------AERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEV 742


                  ..
gi 1720421324 353 MA 354
Cdd:pfam10174 743 MA 744
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 144-283 6.61e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 207
Cdd:COG1579    30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 208 TQKLDLMTEVSELKLKLvgmekeqkeqeekqRKAEELLQELK-HLKIKVEELENERNQYEWELKATKAEVAQLQEQV 283
Cdd:COG1579   110 DEILELMERIEELEEEL--------------AELEAELAELEaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 239-356 7.98e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 239 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHrlk 318
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE--- 322

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720421324 319 mgmETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQ 356
Cdd:COG1196   323 ---EELAELEEELEELEEELEELEEELEEAEEELEEAE 357
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
239-390 8.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 239 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS-------------AALHS 305
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekaeeyiklSEFYE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 306 DHAERDQEIHRLK-------MGMETLLVANEDKDRRIEELTGLLNKYLRVKEIVMATQGPSERTLSInEDEIEGsfRKWN 378
Cdd:PRK03918  304 EYLDELREIEKRLsrleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELER--LKKR 380

                         170
                  ....*....|..
gi 1720421324 379 TTNKSPEEVPKQ 390
Cdd:PRK03918  381 LTGLTPEKLEKE 392
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 146-197 8.43e-04

Protein of unknown function DUF16; The function of this protein is unknown. It appears to only occur in Mycoplasma pneumoniae. The crystal structure revealed that this domain is composed of two separated homotrimeric coiled-coils.


Pssm-ID: 396208 [Multi-domain]  Cd Length: 95  Bit Score: 39.43  E-value: 8.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 146 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 197
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 164-344 9.74e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 164 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEE 243
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI----------EKLKKENQS 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 244 LLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAErdqEIHRLKMGMET 323
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN---QDSVKELIIKN 458

                         170       180
                  ....*....|....*....|.
gi 1720421324 324 LLVANEDKDRRIEELTGLLNK 344
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINK 479
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 149-322 1.22e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  149 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 228
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  229 KEQKEQEEKQRKAEEllqELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDA--------------EIERLH 294
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720421324  295 SQLSRS----AALHSDHAERDQEIHRLKMGME 322
Cdd:pfam01576  306 TELEDTldttAAQQELRSKREQEVTELKKALE 337
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
127-347 1.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 127 DSLSQVNHHGAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSL 206
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGV 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 207 ET------------QKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKaEELLQELKHLKIKVEELENERNQYEWELKATKA 274
Cdd:COG4717   382 EDeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEA 460

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421324 275 EVAQLQEQVAL--KDAEIERLHSQLsrsaalhsdhAERDQEIHRLKMGMETLLVANED-KDRRIEELTGLLNKYLR 347
Cdd:COG4717   461 ELEQLEEDGELaeLLQELEELKAEL----------RELAEEWAALKLALELLEEAREEyREERLPPVLERASEYFS 526
PTZ00121 PTZ00121
MAEBL; Provisional
 171-338 1.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  171 QGEKIRDLEVCLEGHQVKLNAAEEMLQQELlsrtslETQKLDLMTEVSELKLKLVGMEKEQKeqeEKQRKAEELLQELKH 250
Cdd:PTZ00121  1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEE------AKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEE 1658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  251 LKIKVEEL----ENERNQYEwELKATKAEVAQLQEQVAlKDAEIERLHSQLSRSAALHSDHAE---RDQEIHRLKmgMET 323
Cdd:PTZ00121  1659 NKIKAAEEakkaEEDKKKAE-EAKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIK--AEE 1734

                          170
                   ....*....|....*
gi 1720421324  324 LLVANEDKDRRIEEL 338
Cdd:PTZ00121  1735 AKKEAEEDKKKAEEA 1749
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-338 1.76e-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: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlmteVSELKLK 223
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-------LALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 LVGMEKEQKEQEEKQRKAEELLQELKH----LKIKVEELENE--------RNQYEWELKATKAEVAQLQEQVALKDAEIE 291
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREklaqLELRLEGLEVRidnlqerlSEEYSLTLEEAEALENKIEDDEEEARRRLK 975

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324  292 RLHSQLSR-----SAAL--HSDHAER----DQEIHRLKMGMETLLVANEDKDRRIEEL 338
Cdd:TIGR02168  976 RLENKIKElgpvnLAAIeeYEELKERydflTAQKEDLTEAKETLEEAIEEIDREARER 1033
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 677-711 1.88e-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: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720421324 677 VTRWLDDIGLPQYKDQF-HESRVDGRMLQYLTVNDL 711
Cdd:cd09515     9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 598-646 1.93e-03

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 37.66  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720421324 598 AQWSTERVCTWME--DFGLGQYVIFARQWVTSGHTLLTATPQDMEkELGIK 646
Cdd:cd09511     2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-319 2.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  141 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEML------------QQELLSRtSLET 208
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedleeqieelseDIESLAA-EIEE 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  209 QKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENER-------NQYEWELKATKAEVAQLQE 281
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelreklAQLELRLEGLEVRIDNLQE 943

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720421324  282 QVAlKDAEIErLHSQLSRSAALHSDHAERDQEIHRLKM 319
Cdd:TIGR02168  944 RLS-EEYSLT-LEEAEALENKIEDDEEEARRRLKRLEN 979
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 94-339 2.49e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   94 RLALEMLALPQEREALLSQVPGPTATYIKEWFEDSLSQVNhhgaASNETYQERLARLEGDKESLILQVSVLTDQVEAQGE 173
Cdd:TIGR00618  640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ----LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  174 KIRDL-EVCLEGH--QVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqkeqeekqrkAEELLQELKH 250
Cdd:TIGR00618  716 YDREFnEIENASSslGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA-------------ALQTGAELSH 782

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  251 LKIKVEELENERNQYEWELKATKAEVAQlqeqvALKDAEIERL---HSQLSRSAALHSDHAERDQEIHRLKmgmeTLLVA 327
Cdd:TIGR00618  783 LAAEIQFFNRLREEDTHLLKTLEAEIGQ-----EIPSDEDILNlqcETLVQEEEQFLSRLEEKSATLGEIT----HQLLK 853

                          250
                   ....*....|..
gi 1720421324  328 NEDKDRRIEELT 339
Cdd:TIGR00618  854 YEECSKQLAQLT 865
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-347 2.55e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  240 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAALHSDHAERDQEIHRLKM 319
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100
                   ....*....|....*....|....*...
gi 1720421324  320 GMETLLVANEDKdrrIEELTGLLNKYLR 347
Cdd:TIGR02168  772 EAEEELAEAEAE---IEELEAQIEQLKE 796
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 144-373 2.59e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 144 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVklnaaeemlqqellsrtsleTQKLDLMTEVSELKlk 223
Cdd:COG5185   274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQ--------------------LAAAEAEQELEESK-- 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 224 lvgmekeqkeqeekqRKAEELLQELKHlkikveELENERNQYEWELKATKAEVAQLQEQVAL--KDAEIERLHSQLSRSa 301
Cdd:COG5185   332 ---------------RETETGIQNLTA------EIEQGQESLTENLEAIKEEIENIVGEVELskSSEELDSFKDTIEST- 389

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 302 alhsdhAERDQEIHRLKMGMETLLVANEDK-----DRRIEELTGLLNKYLRVKEIVMATQGPSERTLSINEDEIEGS 373
Cdd:COG5185   390 ------KESLDEIPQNQRGYAQEILATLEDtlkaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEE 460
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 239-297 3.33e-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: 38.36  E-value: 3.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421324 239 RKAEELLQELKHLKIKVEElenERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 297
Cdd:pfam20492  58 QEAEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 239-300 3.36e-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: 40.29  E-value: 3.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 239 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS 300
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
144-347 3.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  144 QERLARLEGdkeslilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqelLSRTSLETQKLDlmTEVSELKLK 223
Cdd:COG4913    609 RAKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDVASAE--REIAELEAE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  224 LvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSAAL 303
Cdd:COG4913    677 L--------------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421324  304 HSDHAERDQEIHRLKMGMETLL------------VANEDKDRRIEELTGLLNKYLR 347
Cdd:COG4913    743 ARLELRALLEERFAAALGDAVErelrenleeridALRARLNRAEEELERAMRAFNR 798
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 125-295 4.20e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 125 FEDSLSQVNHHGAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRT 204
Cdd:pfam05557  53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 205 SLETQKLDLMTEVSELKLKLVGMEKEQKEQeekqrkaEELLQELKHLKIKVEELENERNQYE-W--ELKATKAEVAQLQE 281
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDseIVKNSKSELARIPE 201

                         170
                  ....*....|....
gi 1720421324 282 QvalkDAEIERLHS 295
Cdd:pfam05557 202 L----EKELERLRE 211
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 674-732 4.95e-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: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 674 HIW----VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 732
Cdd:cd09575     3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-391 5.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 104 QEREALLSQVPGpTATYIKEWfeDSLSQVNHHGAASNETYQERLARlEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLE 183
Cdd:PRK03918  145 ESREKVVRQILG-LDDYENAY--KNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELR 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 184 GHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEE---LEN 260
Cdd:PRK03918  221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSE 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 261 ERNQYEWELKATKAEVAQLQEQValkdAEIERLHSQLSrsaalhsdhaERDQEIHRLKMGMETLLvanedkdRRIEELTG 340
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEEI----NGIEERIKELE----------EKEERLEELKKKLKELE-------KRLEELEE 359

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720421324 341 LLNKYLRVKEIVMATQGPSERTLSINEDEIEgsfRKWNTTNKSPEEVPKQE 391
Cdd:PRK03918  360 RHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEI 407
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
145-342 5.70e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 145 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsletqkLDLMTEVSELK 221
Cdd:COG4717    71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQL------------LPLYQELEALE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 222 LKLVGMEkeqkeqeekqRKAEELLQELKHLkikvEELENERNQYEWELKATKAEVAQLQEQVALkdAEIERLHSQLSRSA 301
Cdd:COG4717   139 AELAELP----------ERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELE 202

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720421324 302 ALHSDHAERDQEIHRLKMGMETL---------LVANEDKDRRIEELTGLL 342
Cdd:COG4717   203 ELQQRLAELEEELEEAQEELEELeeeleqlenELEAAALEERLKEARLLL 252
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 455-500 5.88e-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: 36.58  E-value: 5.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720421324 455 QKYPTLPGKLSGaTPNGEAAKSPPTASLQPDSSGSSQpklNRGWSV 500
Cdd:cd22296    12 QKYSSESKAEIG-ELARSTQLPFPTPSLSRSTSRSSS---HRGWEI 53
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
191-324 6.40e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 191 AAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELK 270
Cdd:COG4372    28 ALSEQLRKALFELDKLQEELEQLREELEQAREEL---EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421324 271 ATKAEVAQLQEQVALKDAEIERLHSQLSR----SAALHSDHAERDQEIHRLKMGMETL 324
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQleaqIAELQSEIAEREEELKELEEQLESL 162
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 594-645 6.53e-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: 6.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720421324 594 NAPFAQWSTERVCTWMEDFGLGQYV-IFARQWVTsGHTLLTATPQDMeKELGI 645
Cdd:cd09512     1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNID-GQQLLQLDSSKL-KALGI 51
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 677-711 6.93e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.13  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1720421324 677 VTRWLDDIGLPQYKDQFHESRVDGRMLQYLTVNDL 711
Cdd:cd09501     9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDEL 43
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 600-645 7.01e-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: 7.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720421324 600 WSTERVCTWMEDFGLGQYVI--FARQWVTsGHTLLTATPQDMeKELGI 645
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSVCekFRENEIT-GDILLELDLEDL-KELDI 48
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 596-661 7.06e-03

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.08  E-value: 7.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421324 596 PFAQWSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 661
Cdd:cd09575     1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 600-654 7.07e-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: 7.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421324 600 WSTERVCTWMEDFGLGQYV-IFARQWVtSGHTLLTATPQDMEKELGIKHPLHRKKL 654
Cdd:cd09501     4 WSVADVQTWLKQIGFEDYAeKFSESQV-DGDLLLQLTEDELKQDLGMSSGLLRKRF 58
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-293 7.35e-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: 7.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324   90 IEDLRLALEMLalpqEREALLSQVPGPTATY--IKEWFEDSLSQVNHHGAASNETYQERlARLEGDKESLILQVSVLTDQ 167
Cdd:TIGR02169  774 LHKLEEALNDL----EARLSHSRIPEIQAELskLEEEVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQ 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324  168 VEAQGEKIRDLEVCLEghqvKLNAAEEMLQQELLSrtsLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEEL--- 244
Cdd:TIGR02169  849 IKSIEKEIENLNGKKE----ELEEELEELEAALRD---LESRLGDLKKERDELEAQL----------RELERKIEELeaq 911

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421324  245 LQELKH----LKIKVEELENERNQYEWELKATKAEVA------QLQEQVALKDAEIERL 293
Cdd:TIGR02169  912 IEKKRKrlseLKAKLEALEEELSEIEDPKGEDEEIPEeelsleDVQAELQRVEEEIRAL 970
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-345 9.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 141 ETYQERLARLEGDKESL---ILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLN----AAEEMLQQELLSRTSLETQKLDL 213
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLEL 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 214 MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKatKAEVAQLQEQVALKDAEIERL 293
Cdd:PRK03918  608 KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEEL 685

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720421324 294 HSQLSRSAALHSDHAERDQEIHRLKMGMETLLVANEdkdrRIEELTGLLNKY 345
Cdd:PRK03918  686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE----RVEELREKVKKY 733
PRK09039 PRK09039
peptidoglycan -binding protein;
195-350 9.25e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 9.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 195 MLQQELLSRT-SLETQKLD-LMTEVSEL-------KLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQY 265
Cdd:PRK09039   38 VVAQFFLSREiSGKDSALDrLNSQIAELadllsleRQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421324 266 EWELKATKAEVAQL----QEQVALKDAEIERLHSQLSRSAALHSDHAERDQEihrlkmgmetllvanedKDRRIEELTGL 341
Cdd:PRK09039  118 AGELAQELDSEKQVsaraLAQVELLNQQIAALRRQLAALEAALDASEKRDRE-----------------SQAKIADLGRR 180

                         170
                  ....*....|.
gi 1720421324 342 LNKYL--RVKE 350
Cdd:PRK09039  181 LNVALaqRVQE 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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