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Conserved domains on  [gi|1034581973|ref|XP_016875558|]
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liprin-beta-1 isoform X21 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 783-854 6.16e-46

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: 158.77  E-value: 6.16e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 783 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 854
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 ...
 698-760 6.50e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.51  E-value: 6.50e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 698 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
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 ...
 624-687 3.09e-34

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: 125.03  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 624 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 687
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-321 1.96e-08

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.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 58.58  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483 187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 134 IRDLEFCLEEHREKVNATEE--MLQQELLSR---------TSLETQKLDLMAEISNLK-------------LKLTAVEKD 189
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEktKLQDENLKEliekkdhltKELEDIKMSLQRSMSTQKaleedlqiatktiCQLTEEKEA 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 190 RLDYEDKFRDTEGLIqeINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQeklvcKMKGegveivD 269
Cdd:pfam05483 336 QMEELNKAKAAHSFV--VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-----KFKN------N 402

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 270 RDIEVQKMKKAV---ESLMAANEEKDRKIEDLRqclnryKKMQDTVVLAQGKDGE 321
Cdd:pfam05483 403 KEVELEELKKILaedEKLLDEKKQFEKIAEELK------GKEQELIFLLQAREKE 451
 
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 ...
 783-854 6.16e-46

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: 158.77  E-value: 6.16e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 783 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 854
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 ...
 698-760 6.50e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.51  E-value: 6.50e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 698 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
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 ...
 624-687 3.09e-34

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: 125.03  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 624 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 687
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 700-760 1.75e-18

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: 80.01  E-value: 1.75e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 700 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 626-688 8.31e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 8.31e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 626 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 688
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 624-688 3.83e-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: 62.31  E-value: 3.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973  624 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 688
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 700-760 1.18e-11

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: 60.77  E-value: 1.18e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973  700 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
787-854 4.08e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.08e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 787 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 854
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-321 1.96e-08

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: 58.58  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483 187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 134 IRDLEFCLEEHREKVNATEE--MLQQELLSR---------TSLETQKLDLMAEISNLK-------------LKLTAVEKD 189
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEktKLQDENLKEliekkdhltKELEDIKMSLQRSMSTQKaleedlqiatktiCQLTEEKEA 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 190 RLDYEDKFRDTEGLIqeINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQeklvcKMKGegveivD 269
Cdd:pfam05483 336 QMEELNKAKAAHSFV--VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-----KFKN------N 402

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 270 RDIEVQKMKKAV---ESLMAANEEKDRKIEDLRqclnryKKMQDTVVLAQGKDGE 321
Cdd:pfam05483 403 KEVELEELKKILaedEKLLDEKKQFEKIAEELK------GKEQELIFLLQAREKE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-307 2.57e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQqELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 184 TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserlqyEKKLKSTKDELASLKEQLEEKEsEVKRLQ---EKLVCKM 260
Cdd:PRK03918  310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYE-EAKAKKeelERLKKRL 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 261 KGEGVEIVDRDIE-VQKMKKAVE----SLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:PRK03918  382 TGLTPEKLEKELEeLEKAKEEIEeeisKITARIGELKKEIKELKKAIEELKK 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-307 3.70e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---VNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973  242 LEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:TIGR02168  423 IEELLKKLEEAELKEL------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-308 2.74e-07

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: 52.62  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 207 INDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrDIEVQKMKKAVESLMA 286
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL--------------DEELAELEAELEELEA 163

                         170       180
                  ....*....|....*....|...
gi 1034581973 287 ANEEKDRKI-EDLrqcLNRYKKM 308
Cdd:COG1579   164 EREELAAKIpPEL---LALYERI 183
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 784-853 9.98e-07

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: 46.91  E-value: 9.98e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  784 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 853
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
 
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 ...
 783-854 6.16e-46

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: 158.77  E-value: 6.16e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 783 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 854
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 ...
 698-760 6.50e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.51  E-value: 6.50e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 698 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
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 ...
 624-687 3.09e-34

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: 125.03  E-value: 3.09e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 624 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 687
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 ...
 791-852 3.44e-33

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: 121.88  E-value: 3.44e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 791 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 852
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 ...
 787-854 2.33e-31

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: 117.16  E-value: 2.33e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 787 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 854
Cdd:cd09570     5 WTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 703-760 1.75e-20

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: 85.66  E-value: 1.75e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973 703 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 760
Cdd:cd09495     2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 700-760 1.75e-18

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: 80.01  E-value: 1.75e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 700 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
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 ...
 787-854 6.55e-18

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: 78.90  E-value: 6.55e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 787 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 854
Cdd:cd09568     5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 626-688 8.31e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 8.31e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 626 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 688
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 632-687 3.79e-14

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: 67.64  E-value: 3.79e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 632 VCNWLMEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 687
Cdd:cd09494     2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 703-757 5.45e-13

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: 64.18  E-value: 5.45e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 703 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 757
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 698-760 9.43e-13

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: 63.97  E-value: 9.43e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 698 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 760
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 624-688 3.83e-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: 62.31  E-value: 3.83e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973  624 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 688
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 700-760 1.18e-11

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: 60.77  E-value: 1.18e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973  700 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
787-854 4.08e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.08e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 787 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 854
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 631-686 6.24e-09

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: 52.63  E-value: 6.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973 631 QVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 686
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-321 1.96e-08

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: 58.58  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483 187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 134 IRDLEFCLEEHREKVNATEE--MLQQELLSR---------TSLETQKLDLMAEISNLK-------------LKLTAVEKD 189
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEktKLQDENLKEliekkdhltKELEDIKMSLQRSMSTQKaleedlqiatktiCQLTEEKEA 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 190 RLDYEDKFRDTEGLIqeINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQeklvcKMKGegveivD 269
Cdd:pfam05483 336 QMEELNKAKAAHSFV--VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-----KFKN------N 402

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 270 RDIEVQKMKKAV---ESLMAANEEKDRKIEDLRqclnryKKMQDTVVLAQGKDGE 321
Cdd:pfam05483 403 KEVELEELKKILaedEKLLDEKKQFEKIAEELK------GKEQELIFLLQAREKE 451
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-307 2.57e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQqELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 184 TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserlqyEKKLKSTKDELASLKEQLEEKEsEVKRLQ---EKLVCKM 260
Cdd:PRK03918  310 REIEKRLSRLEEEINGIEERIKELEEKEERLEEL-------KKKLKELEKRLEELEERHELYE-EAKAKKeelERLKKRL 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 261 KGEGVEIVDRDIE-VQKMKKAVE----SLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:PRK03918  382 TGLTPEKLEKELEeLEKAKEEIEeeisKITARIGELKKEIKELKKAIEELKK 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-307 3.70e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---VNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973  242 LEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:TIGR02168  423 IEELLKKLEEAELKEL------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
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 ...
 699-761 3.79e-08

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: 50.93  E-value: 3.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 699 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 761
Cdd:cd09565     1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-298 6.66e-08

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: 56.57  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 LTAVEKDrldYEDKFRDTEGLIQEINDLRLKVSEMDSErlqyEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKG 262
Cdd:TIGR04523 484 LEQKQKE---LKSKEKELKKLNEEKKELEEKVKDLTKK----ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034581973 263 EGVEIVDRDI--EVQKMKKAVESLMAANEEKDRKIEDL 298
Cdd:TIGR04523 557 ENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQK 594
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-318 2.24e-07

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: 55.06  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSV-------LTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  176 ISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEIndlrlkvsemdserlqyEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDL-----------------EEQIEELSEDIESLAAEIEELEELIEELESE 874

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973  256 LvckmKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGK 318
Cdd:TIGR02168  875 L----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 625-686 2.26e-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: 48.99  E-value: 2.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 625 AKWTKEQVCNWL-MEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 686
Cdd:cd09564     2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-324 2.56e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 131 GEKIRDLEFCLEEHREKVNATEEMlqQELLSrtSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDL 210
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENI--EELIK--EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 211 RLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQE-----KLVCKMKGEGVEIVDRDIEVQKMK------- 278
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLsrleeei 323

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034581973 279 KAVESLMAANEEKDRKIEDLRqclNRYKKMQDTVVLAQGKDGEYEE 324
Cdd:PRK03918  324 NGIEERIKELEEKEERLEELK---KKLKELEKRLEELEERHELYEE 366
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-308 2.74e-07

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: 52.62  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 207 INDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrDIEVQKMKKAVESLMA 286
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL--------------DEELAELEAELEELEA 163

                         170       180
                  ....*....|....*....|...
gi 1034581973 287 ANEEKDRKI-EDLrqcLNRYKKM 308
Cdd:COG1579   164 EREELAAKIpPEL---LALYERI 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-300 2.83e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ------ELLSRTSLET 167
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  168 QK--LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQ 241
Cdd:TIGR02169  293 KEkiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDkllaEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973  242 LEEKESEVKRLQEKLvckmkgegveiVDRDIEVQKMKKAVESLmaaNEEKDRKIEDLRQ 300
Cdd:TIGR02169  373 LEEVDKEFAETRDEL-----------KDYREKLEKLKREINEL---KRELDRLQEELQR 417
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 704-759 4.38e-07

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: 48.08  E-value: 4.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973 704 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 759
Cdd:cd09506    10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-320 5.85e-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: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDK--------------ESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQ 168
Cdd:COG1196   294 LAELARLEQDIarleerrreleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 169 KLDLMAEISNLKLKLTAVEKDRLDYEDKfrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESE 248
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 249 VKRLQEKLvckmKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDG 320
Cdd:COG1196   451 EAELEEEE----EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 784-853 9.98e-07

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: 46.91  E-value: 9.98e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  784 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 853
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 704-756 1.08e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.54  E-value: 1.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 704 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 756
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
700-760 1.46e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.49  E-value: 1.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 700 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:pfam07647   5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 102-482 1.94e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 51.97  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  102 YQERLARLENDKESLVlqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELlsrtslETQKLDLMAEISNLKL 181
Cdd:PTZ00108   986 YLVRLDLYKKRKEYLL---GKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKEL------KKLGYVRFKDIIKKKS 1056

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  182 KLTAVEKDrldyEDKFRDTEGLIQEINDLRLKVSEMDserlqY--EKKLKS-TKDELASLKEQLEEKESEVKRLQEKLVC 258
Cdd:PTZ00108  1057 EKITAEEE----EGAEEDDEADDEDDEEELGAAVSYD-----YllSMPIWSlTKEKVEKLNAELEKKEKELEKLKNTTPK 1127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  259 KMKGEGVEIVDRDIEVQKMKKAVESlmaANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDGEYEELLNSSSISSLLDAQ 338
Cdd:PTZ00108  1128 DMWLEDLDKFEEALEEQEEVEEKEI---AKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSD 1204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  339 GFSDLEKSPSPTPVMGSPSCDPFN----------------------TSVPEEFHTTILQVSIPSLLPATVSMETSEKSKL 396
Cdd:PTZ00108  1205 EKRKLDDKPDNKKSNSSGSDQEDDeeqktkpkkssvkrlkskknnsSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYS 1284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  397 TPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNLKKETSDGEKetiqKTSEDRAPAESRPFGTLPPRPPG 475
Cdd:PTZ00108  1285 PPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKS----KTRVKQASASQSSRLLRRPRKKK 1360


                   ....*..
gi 1034581973  476 QDTSMDD 482
Cdd:PTZ00108  1361 SDSSSED 1367
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-300 2.44e-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: 51.60  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvcKMKG 262
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL--EELE 322

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034581973  263 EGVEIVDRDIEVQKMKKA------------VESLMAANEEKDRKIEDLRQ 300
Cdd:TIGR02168  323 AQLEELESKLDELAEELAeleekleelkeeLESLEAELEELEAELEELES 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-295 2.49e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQEL--LSRTSLETQKLDLMAEISNLK 180
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraLYRSGGSVSYLDVLLGSESFS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 181 lklTAVekDRLDYEDKFRDTEG-LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvck 259
Cdd:COG3883   116 ---DFL--DRLSALSKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL--- 187

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034581973 260 mkgegveivdrDIEVQKMKKAVESLMAANEEKDRKI 295
Cdd:COG3883   188 -----------SAEEAAAEAQLAELEAELAAAEAAA 212
Filament pfam00038
Intermediate filament protein;
125-256 2.51e-06

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 50.69  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 125 DQVEAQGEKIRDLEFCLEEHREK----VNATEEMLQQEL--LSRT--SLETQKLDLMAEISNLKLkltAVEKDRLDYEDK 196
Cdd:pfam00038  18 DKVRFLEQQNKLLETKISELRQKkgaePSRLYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 197 FRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEkesEVKRLQEKL 256
Cdd:pfam00038  95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEE---EVRELQAQV 151
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 627-688 3.87e-06

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 45.39  E-value: 3.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 627 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 688
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-307 4.79e-06

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: 48.77  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKD- 233
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNn 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 234 --------ELASLKEQLEEKESEVKRLQEKLvckmkgEGVEIVDRDIEvQKMKKAVESLMAANEEKDRKIEDLRQCLNRY 305
Cdd:COG1579    89 keyealqkEIESLKRRISDLEDEILELMERI------EELEEELAELE-AELAELEAELEEKKAELDEELAELEAELEEL 161


                  ..
gi 1034581973 306 KK 307
Cdd:COG1579   162 EA 163
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-304 5.57e-06

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: 49.76  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 129 AQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTE----GLI 204
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiaELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 205 QEINDLRLKVSEM-----------------------DSER-LQYEK-----------KLKSTKDELASLKEQLEEKESEV 249
Cdd:COG4942    97 AELEAQKEELAELlralyrlgrqpplalllspedflDAVRrLQYLKylaparreqaeELRADLAELAALRAELEAERAEL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 250 KRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 304
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-300 6.05e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 102 YQERLARLenDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:COG1196   218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMK 261
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034581973 262 GEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 300
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 89-300 7.69e-06

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: 50.11  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  89 QMTNghLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQ 168
Cdd:pfam05483 395 EMTK--FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 169 KLDLMAEISNLKLK---LTAvEKDRLDYEDKfrdteGLIQEINDLRLKV----SEMDSERLQYEKKLKST---------- 231
Cdd:pfam05483 473 VEDLKTELEKEKLKnieLTA-HCDKLLLENK-----ELTQEASDMTLELkkhqEDIINCKKQEERMLKQIenleekemnl 546

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973 232 KDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 300
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-307 7.79e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 125 DQVEAQGEKIRDLEFCLEEHREKVNATEEmlqqellsrtsLETQKLDLMAEISNLKLKLTAVEKDRLDYEdkfrdtegLI 204
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEE-----------LEEELEELEAELEELREELEKLEKLLQLLP--------LY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 205 QEINDLRLKVSEMDsERLQyekKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDrdiEVQKMKKAVESL 284
Cdd:COG4717   132 QELEALEAELAELP-ERLE---ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEEL 204

                         170       180
                  ....*....|....*....|...
gi 1034581973 285 MAANEEKDRKIEDLRQCLNRYKK 307
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEE 227
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
76-300 8.36e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  76 DSTAETLVEW-LQSQMTNGhlpgNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM 154
Cdd:PRK02224  324 EELRDRLEECrVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE------------------INDLRLKVSE 216
Cdd:PRK02224  400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEE 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 217 MDSERLQYEKKLKSTKDELASLkEQLEEKESEVKRLQEK--LVCKMKGEGVEIVDRDIE-VQKMKKAVESLMAANEEKDR 293
Cdd:PRK02224  480 LEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERreDLEELIAERRETIEEKRErAEELRERAAELEAEAEEKRE 558


                  ....*..
gi 1034581973 294 KIEDLRQ 300
Cdd:PRK02224  559 AAAEAEE 565
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-239 8.76e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 8.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAE 175
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLEREIerleRELEERERRRARLEAL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973  176 ISNLKLKLTAVEKDRLDYEDKFRDT-EGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLK 239
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALlEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 102-313 9.69e-06

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: 49.35  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSL-------ETQKLDLMA 174
Cdd:pfam05557  25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALnkklnekESQLADARE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 175 EISNLKLKL----TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVk 250
Cdd:pfam05557 105 VISCLKNELselrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE- 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 251 rlQEKLVCK-MKGEGVEIVDRDIEVQKMKKAVESLMAANEEK---DRKIEDLRQCLNRYKKMQDTVV 313
Cdd:pfam05557 184 --QDSEIVKnSKSELARIPELEKELERLREHNKHLNENIENKlllKEEVEDLKRKLEREEKYREEAA 248
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-272 1.09e-05

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: 48.00  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellSRTSLETQklDLMAEISNLKLK 182
Cdd:COG1579    30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---VRNNKEYE--ALQKEIESLKRR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 LTAVEKDRLDYEDKFRDTEGLIQEIND-LRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEV----KRLQEKLV 257
Cdd:COG1579   105 ISDLEDEILELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIppelLALYERIR 184

                         170
                  ....*....|....*
gi 1034581973 258 CKMKGEGVEIVDRDI 272
Cdd:COG1579   185 KRKNGLAVVPVEGGA 199
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-300 1.12e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--VNATEEMLQQELLSRTSLETQKLDLMAEIS 177
Cdd:COG3206   159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 178 NLKLKLTAVEKDRLDYEDKFRDTEGlIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLV 257
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034581973 258 CKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 300
Cdd:COG3206   316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLER 358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-255 1.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQG--EKIRDLEFCLEEHREKVnateEMLQQELLSRTSLETQKLDLMAEISNLK 180
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQ 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 181 LKLTAVEKdrldyedkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:COG4717   177 EELEELLE---------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
103-256 1.36e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKlk 182
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR-- 327

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 183 lTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:PRK02224  328 -DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 87-313 1.67e-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: 48.96  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973   87 QSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEA-QGEKIRDLEFCLEEHREKVNA------------TE- 152
Cdd:pfam15921  207 HDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQliseheveitglTEk 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  153 ---------------EMLQQELLSRTSLETQKL-DLMAEISNLKLKLTavEKDRLdYEDKFRDTEGLIQEINDlrlKVSE 216
Cdd:pfam15921  287 assarsqansiqsqlEIIQEQARNQNSMYMRQLsDLESTVSQLRSELR--EAKRM-YEDKIEELEKQLVLANS---ELTE 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  217 MDSERLQYEKKLKSTKDELASLKEQLEEKESEV---KRLQEKLVCKMKGEGV-------EIVDRDIEVQKMKKAVESL-- 284
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDRDTGNSItidhlrrELDDRNMEVQRLEALLKAMks 440

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034581973  285 ---------MAANEEKD---RKIEDLRQCLNRYKKMQDTVV 313
Cdd:pfam15921  441 ecqgqmerqMAAIQGKNeslEKVSSLTAQLESTKEMLRKVV 481
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-302 1.69e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  109 LENDKESLVLQVSVLTdQVEAQGE-KIRDLEFCLEEHREKVNATEEmLQQELLSRTSLETQKLD-LMAEISNLKLKLTAV 186
Cdd:pfam01576  382 LESENAELQAELRTLQ-QAKQDSEhKRKKLEGQLQELQARLSESER-QRAELAEKLSKLQSELEsVSSLLNEAEGKNIKL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  187 EKDRLDYEDKFRDTEGLIQEinDLRLKvsemdserLQYEKKLKSTKDELASLKEQLEEkESEVKRLQEKLVCKMKgegVE 266
Cdd:pfam01576  460 SKDVSSLESQLQDTQELLQE--ETRQK--------LNLSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQLSTLQ---AQ 525

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034581973  267 IVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCL 302
Cdd:pfam01576  526 LSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
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 ...
 624-688 2.46e-05

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: 43.32  E-value: 2.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 624 FAKWTKEQVCNWL-MEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 688
Cdd:cd09562     1 FALWNGPTVVAWLeLWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 104-310 2.85e-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: 48.14  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleEHREKVNATEEMLQQELlsrTSLETQKLDLMAEISNLKLKL 183
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKK---EELEEELEELEAALRDLESRL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  184 TAVEKDRLDYEDKFRDTEGLIQEINdlrlkvsemdserLQYEKKlkstKDELASLKEQLEEKESEVKRLQEKlvckmKGE 263
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELE-------------AQIEKK----RKRLSELKAKLEALEEELSEIEDP-----KGE 942

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034581973  264 GVEIV--DRDIE-VQKMKKAVESLMAANEEKD-RKIEDLRQCLNRYKKMQD 310
Cdd:TIGR02169  943 DEEIPeeELSLEdVQAELQRVEEEIRALEPVNmLAIQEYEEVLKRLDELKE 993
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-307 3.93e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQEllsrtSLETQKLDLMAEISNLKL- 181
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDAs 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  182 --KLTAVEKDRldyedkfrdtEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCK 259
Cdd:COG4913    684 sdDLAALEEQL----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581973  260 MKGegvEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:COG4913    754 RFA---AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 701-759 4.26e-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: 42.31  E-value: 4.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 701 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 759
Cdd:cd09530     1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-256 5.41e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 5.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  132 EKIRDLEFCLEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1034581973  208 ndLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKL 256
Cdd:pfam01576  417 --LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
627-688 5.60e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 5.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 627 WTKEQVCNWLMEQGLGSYLNS-GKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 688
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 623-688 7.25e-05

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: 41.63  E-value: 7.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 623 PFAKWTKEQVCNWLMEQGLGSYLNS-GKHWIaSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 688
Cdd:cd09507     1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-253 1.08e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKVNATEEMLQQELLsrtSLETQKLD-LMAEISNLKL 181
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIR---GNGGDRLEqLEREIERLER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  182 KLTAVEKDRLDYEDKFR--------DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQ 253
Cdd:COG4913    353 ELEERERRRARLEALLAalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-307 1.15e-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: 46.17  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEisnLKLKLTAVEK 188
Cdd:TIGR04523 300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 189 DRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELAS-------LKEQLEEKESEVKRLQEklvckmk 261
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELlekeierLKETIIKNNSEIKDLTN------- 447

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034581973 262 gegvEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:TIGR04523 448 ----QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 161-312 1.62e-04

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: 45.14  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 161 SRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKE 240
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 241 QLEEKESEVKRL---------QEKLVCKMKGEGVEIVDRDIE-----VQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 306
Cdd:COG4942    98 ELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAELE 177


                  ....*.
gi 1034581973 307 KMQDTV 312
Cdd:COG4942   178 ALLAEL 183
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-256 1.66e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  183 LTAVEKDRLDYEdkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKS----TKDELASLKEQLEEKES----EVKRLQE 254
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEearrRLKRLEN 979


                   ..
gi 1034581973  255 KL 256
Cdd:TIGR02168  980 KI 981
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 627-688 1.83e-04

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: 40.75  E-value: 1.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 627 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 688
Cdd:cd09501     4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-297 1.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLK 182
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-------LNEQLQAAQAELAQAQEE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 LTAVEKDrldYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKG 262
Cdd:COG4372   103 LESLQEE---AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034581973 263 EGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIED 297
Cdd:COG4372   180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 2.14e-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: 41.35  E-value: 2.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQ 156
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 119-324 2.32e-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: 45.20  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATE------------------------EMLQQEllsRTSLETQKLD--- 171
Cdd:pfam10174 395 KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQtdssntdtalttleealsekeriiERLKEQ---REREDRERLEele 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 172 -LMAEISNLKLKLTAVEKDRLDYEdkfrdtegliQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVK 250
Cdd:pfam10174 472 sLKKENKDLKEKVSALQPELTEKE----------SSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 251 RLQEKLVCKMKGEgvEIVDR----DIEVQ-------KMKKAVESLMAANEE-------KDRKIEDLRQCLNRYKKMQDTV 312
Cdd:pfam10174 542 KAHNAEEAVRTNP--EINDRirllEQEVArykeesgKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQNKK 619

                         250
                  ....*....|..
gi 1034581973 313 VlAQGKDGEYEE 324
Cdd:pfam10174 620 V-ANIKHGQQEM 630
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 105-309 2.69e-04

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.42  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 105 RLARLENDKESLVLQVSVLTDQveaqgEKIRDLEFCLEEHREKVNATEE--MLQQELLSRTSLETQKlDL---MAEISNL 179
Cdd:pfam15905 130 QLLELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKevMAKQEGMEGKLQVTQK-NLehsKGKVAQL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 180 KLKLTAVEKDRLDYEDkfrDTEGLIQEIndlrlkvSEMDSERLQYEKklksTKDELASLKEQLEEKESEVKRLQEKLVCK 259
Cdd:pfam15905 204 EEKLVSTEKEKIEEKS---ETEKLLEYI-------TELSCVSEQVEK----YKLDIAQLEELLKEKNDEIESLKQSLEEK 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 260 MKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKI--------EDLRQCLNRYKKMQ 309
Cdd:pfam15905 270 EQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLnaeleelkEKLTLEEQEHQKLQ 327
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-300 2.77e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 127 VEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE 206
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 207 IND----LRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvcKMKGEGVEIVDRDIEVQKMKKAVE 282
Cdd:COG4372   106 LQEeaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL--ESLQEELAALEQELQALSEAEAEQ 183

                         170
                  ....*....|....*...
gi 1034581973 283 SLMAANEEKDRKIEDLRQ 300
Cdd:COG4372   184 ALDELLKEANRNAEKEEE 201
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 623-679 2.96e-04

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: 39.94  E-value: 2.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034581973 623 PFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGI-----KHSLHRK 679
Cdd:cd09512     3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 704-761 3.45e-04

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 39.87  E-value: 3.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973 704 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 761
Cdd:cd09547     6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 166-256 3.76e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 166 ETQKLDLMAEISNLKLKLTAVEKdrldyedkfrdtegliqEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEK 245
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQA-----------------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77

                          90
                  ....*....|.
gi 1034581973 246 ESEVKRLQEKL 256
Cdd:COG3883    78 EAEIEERREEL 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-250 4.40e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNAteemlqqellsrtsLETQKLDLMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973  182 KLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVK 250
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-303 4.60e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQveaqgekIRDLEFCLEEHREKvnatEEMLQQELlsrTSLETQKLDLMAEISNLKlk 182
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQ-------INDLESKIQNQEKL----NQQKDEQI---KKLQQEKELLEKEIERLK-- 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 ltaveKDRLDYEDKFRDtegLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRlQEKLVCKMKG 262
Cdd:TIGR04523 433 -----ETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS-KEKELKKLNE 503

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034581973 263 EGVE----IVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLN 303
Cdd:TIGR04523 504 EKKEleekVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 103-284 4.67e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 42.23  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQG-EKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:pfam08614  13 LDRTALLEAENAKLQSEPESVLPSTSSSKlSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 182 KLTAVEKdRLdyedkfrdtEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEklvckmk 261
Cdd:pfam08614  93 KLREDER-RL---------AALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK------- 155

                         170       180
                  ....*....|....*....|...
gi 1034581973 262 gEGVEIVDRdiEVQKMKKAVESL 284
Cdd:pfam08614 156 -ENRELVER--WMKRKGQEAEAM 175
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 701-760 4.99e-04

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 39.60  E-value: 4.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 701 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:cd09552     6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 630-681 5.41e-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: 39.16  E-value: 5.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 630 EQVCNWLMEQGLGSYLNsgkHWIASG---QTLLQASQQDLeKELGIKHSLHRKKL 681
Cdd:cd09497     5 EAIFDWLREFGLEEYTP---NFIKAGydlPTISRMTPEDL-TAIGITKPGHRKKL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
104-300 7.39e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  104 ERLARLENDKESLVLQVSVLT------DQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRtsLETQKLDLMAEIS 177
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--LRAELARLEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  178 NLKLKLTAVEKDRLDYEDKFRDTEG-----LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRL 252
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGGdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034581973  253 QEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLmaaneekDRKIEDLRQ 300
Cdd:COG4913    393 LEALEEELEALEEALAEAEAALRDLRRELREL-------EAEIASLER 433
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 187-306 7.56e-04

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 42.22  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 187 EKDRLDyedkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEekesEVKRLQEKLVCKMkgegVE 266
Cdd:pfam11932  35 KIDKWD-----DEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIE----EIERTERELVPLM----LK 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034581973 267 IVDRdievqkMKKAVESLMAAN-EEKDRKIEDLRQCLNRYK 306
Cdd:pfam11932 102 MLDR------LEQFVALDLPFLlEERQARLARLRELMDDAD 136
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 625-673 9.80e-04

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 38.43  E-value: 9.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 625 AKWTKEQVCNWL--MEQGLGSYLNSGKHWIASGQTLLQASQQDLEkELGIK 673
Cdd:cd09511     2 AKWSPKQVTDWLkgLDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 701-759 1.07e-03

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 38.37  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 701 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 759
Cdd:cd09488     2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-308 1.13e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFC---LEEHREKVNATEEMLQQELLSrtsLETQKlDLMAEI 176
Cdd:COG1340    67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLS---PEEEK-ELVEKI 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 177 SNLKLKLTAVEKdRLDYEDKFRDTEGLIQEI----NDLRLKVSEMDSERLQYEKKLKSTKDELASLK-------EQLEEK 245
Cdd:COG1340   143 KELEKELEKAKK-ALEKNEKLKELRAELKELrkeaEEIHKKIKELAEEAQELHEEMIELYKEADELRkeadelhKEIVEA 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034581973 246 ESEVKRLQEKLVCKMKgegvEIVDRDIEVQKMKKAVESLM--AANEEKDRKIEDLRQCLNRYKKM 308
Cdd:COG1340   222 QEKADELHEEIIELQK----ELRELRKELKKLRKKQRALKreKEKEELEEKAEEIFEKLKKGEKL 282
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 627-668 1.19e-03

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.


Pssm-ID: 188913  Cd Length: 72  Bit Score: 38.62  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034581973 627 WTKEQVCNWLMEQGLGSYLNSGKHWiaSGQTLLQASQQDLEK 668
Cdd:cd09514     7 WSPKEVSDWLSEEGMQEYSEALRSF--DGQALLNLTEEDFKK 46
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 108-306 1.23e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 108 RLEnDKESLVL----QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNateeMLQQELlsrTSLETQKLDLMAEISNLKLKL 183
Cdd:pfam10174 353 RLE-EKESFLNkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN----VLQKKI---ENLQEQLRDKDKQLAGLKERV 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 184 TAVEKDRLDYEDKFRDTEGLIQE----INDLRLKVSEMDSERL----QYEKKLKSTKDELASLKEQLEEKESEVKRLQEK 255
Cdd:pfam10174 425 KSLQTDSSNTDTALTTLEEALSEkeriIERLKEQREREDRERLeeleSLKKENKDLKEKVSALQPELTEKESSLIDLKEH 504

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 256 ---LVCKMKGEGVEIVDRDIEVQK-----------MKKAVESLMAA--NEEKDRKIEDLRQCLNRYK 306
Cdd:pfam10174 505 assLASSGLKKDSKLKSLEIAVEQkkeecsklenqLKKAHNAEEAVrtNPEINDRIRLLEQEVARYK 571
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 625-688 1.35e-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: 38.00  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 625 AKWTKEQVCNWLMEQGLGSYLNS--GKHWIaSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 688
Cdd:cd09515     2 HEWTCEDVAKWLKKEGFSKYVDLlcNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 103-303 1.57e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.73  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  103 QERLARLENDKESLVLQVSVLTDQVEAQGE-------KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLdlmaE 175
Cdd:TIGR01612 1536 KNKFAKTKKDSEIIIKEIKDAHKKFILEAEkseqkikEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFL----K 1611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  176 ISNLKLKLTavekdrldyeDKFRDTEGLIQEIN-------DLRLKVSEMDSERLQ-YEKKLKSTKDELASLKEQLEEKES 247
Cdd:TIGR01612 1612 ISDIKKKIN----------DCLKETESIEKKISsfsidsqDTELKENGDNLNSLQeFLESLKDQKKNIEDKKKELDELDS 1681

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973  248 EVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKavESLMAANEEKDRKIEDLRQCLN 303
Cdd:TIGR01612 1682 EIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK--EEIESIKELIEPTIENLISSFN 1735
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-278 1.59e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEehreKVNATEEMLQQELLSRTS-----------LETQKLD 171
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN----KIKQNLEQKQKELKSKEKelkklneekkeLEEKVKD 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 172 LMAEISNLKLKLTAVEKDRLDYEDKFRDTE--------------------GLIQEINDLRLKVSEMDSERLQYEKKLKST 231
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEdelnkddfelkkenlekeidEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034581973 232 KDELASLKEQLEEKESEVKRLQEKLvckmkgEGVEIVDRDIEVQKMK 278
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKEL------EKAKKENEKLSSIIKN 635
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 627-671 1.64e-03

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188925  Cd Length: 66  Bit Score: 37.72  E-value: 1.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034581973 627 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQ---QDLEKELG 671
Cdd:cd09526     4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 119-355 2.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLKLTAVE---KDRL---- 191
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERReelGERAraly 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 192 ------DYEDKF---RDTEGLIQEINDLRlKVSEMDSERLQyekKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKg 262
Cdd:COG3883    97 rsggsvSYLDVLlgsESFSDFLDRLSALS-KIADADADLLE---ELKADKAELEAKKAELEAKLAELEALKAELEAAKA- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 263 egveivdrdiEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDGEYEELLNSSSISSLLDAQGFSD 342
Cdd:COG3883   172 ----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241

                         250
                  ....*....|...
gi 1034581973 343 LEKSPSPTPVMGS 355
Cdd:COG3883   242 AAASAAGAGAAGA 254
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 203-312 2.03e-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: 41.06  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 203 LIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEV-------KRLQEKLVCKMKGEGVEIVDRDIEVQ 275
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeveariKKYEEQLGNVRNNKEYEALQKEIESL 101

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034581973 276 KMKKAV--ESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 312
Cdd:COG1579   102 KRRISDleDEILELMERIEELEEELAELEAELAELEAEL 140
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 627-683 2.04e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 2.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 627 WTKEQVCNWLMEQ-GLGSYLNSGKHWIASGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 683
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-307 2.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 141 LEEHREKVNATEEMLQQELLSRTSLETQKlDLMAEISNLKLKLTAVEKDRLdyEDKFRDTEGLIQEINDLRLKVS----- 215
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLEEL--EKKAEEYEKLKEKLIKLKGEIKslkke 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 216 -----EMDSERLQYEKKLKSTKDELASLKEQLEEK--------ESEVKRLQE--KLVCKMKGEGVEIVDRDIEVQKMKKA 280
Cdd:PRK03918  548 lekleELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPfyNEYLELKDAEKELEREEKELKKLEEE 627

                         170       180
                  ....*....|....*....|....*..
gi 1034581973 281 VESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:PRK03918  628 LDKAFEELAETEKRLEELRKELEELEK 654
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 783-835 2.51e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 783 EVQKWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 835
Cdd:cd09504     1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 148-281 2.61e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 148 VNATEEMLQQ---ELLSRTSLETQKLDLMAEISNLKLKltavekdrldyedkfrdtegliqeINDLRLKVSEMDSERLQY 224
Cdd:pfam11559  37 INVIYELLQQrdrDLEFRESLNETIRTLEAEIERLQSK------------------------IERLKTQLEDLERELALL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034581973 225 EKKLKSTKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAV 281
Cdd:pfam11559  93 QAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERL 149
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 175-303 2.92e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 175 EIS-NLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRL----KVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEV 249
Cdd:PRK00409  492 EIAkRLGLPENIIEEAKKLIGEDKEKLNELIASLEELEReleqKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034581973 250 KRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAveslmaanEEKDRKIEDLRQCLN 303
Cdd:PRK00409  572 EKEAQQAIKEAKKEADEIIKELRQLQKGGYA--------SVKAHELIEARKRLN 617
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 704-760 3.47e-03

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: 36.91  E-value: 3.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034581973 704 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 760
Cdd:cd09505    10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 108-323 3.59e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 108 RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNaTEEMLQQELLSRtsLETQKldlmAEISNLKLKLTAVE 187
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR-LEEQERQQQVER--LRQQE----EERKRKKLELEKEK 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 188 KDRLDYEDKFRDTegLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELAslkEQLEEKESEVKRLQEKlvckmkgegvei 267
Cdd:pfam17380 484 RDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEKEMEERQKAIY---EEERRREAEEERRKQQ------------ 546

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973 268 vdrdiEVQKMKKAVESLMAANEEKDRkiedlRQCLNRYKKMQDTVVLAQGKDGEYE 323
Cdd:pfam17380 547 -----EMEERRRIQEQMRKATEERSR-----LEAMEREREMMRQIVESEKARAEYE 592
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 701-760 4.03e-03

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 36.77  E-value: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 701 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 760
Cdd:cd09549     7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 85-309 4.99e-03

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 40.82  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  85 WLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQV--------SVLTDQVEAQGEKIRDLE-FCL-----EEHR-EKVN 149
Cdd:COG5244   370 WLSEFLQRKFSSKQETAFSICQFLEDNKDVTLILKIlhpilettVPKLLAFLRTNSNFNDNDtLCLigslyEIARiDKLI 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 150 ATEEMLQQelLSRTSLETQKLdlMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKvsemDSERLQYEKKLK 229
Cdd:COG5244   450 GKEEISKQ--DNRLFLYPSCD--ITLSSILTILFSDKLEVFFQGIESLLENITIFPEQPSQQTS----DSENIKENSLLS 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 230 STKDEL-ASLKEQLEEKESEVkrlQEKLVCKMkgegveIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR-QCLNRYKK 307
Cdd:COG5244   522 DRLNEEnIRLKEVLVQKENML---TEETKIKI------IIGRDLERKTLEENIKTLKVELNNKNNKLKEENfNLVNRLKN 592


                  ..
gi 1034581973 308 MQ 309
Cdd:COG5244   593 ME 594
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-256 5.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 102 YQERLARLENDKESLVLQVSVLTDQVEAQG--------EKIRDLEFCLEEHREKVNATEEmLQQELLSRTSLETQKLDLM 173
Cdd:PRK03918  554 LKKKLAELEKKLDELEEELAELLKELEELGfesveeleERLKELEPFYNEYLELKDAEKE-LEREEKELKKLEEELDKAF 632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 174 AEISNLKLKLTAVEKDRLDYEDKFRDTE--GLIQEINDLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKR 251
Cdd:PRK03918  633 EELAETEKRLEELRKELEELEKKYSEEEyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712


                  ....*
gi 1034581973 252 LqEKL 256
Cdd:PRK03918  713 L-EKL 716
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 103-317 5.62e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 103 QERLARLENDKESLVLQVSVLTDQVeAQGEKIRDLEFCLEEHREKVNATEEmlqqellsRTSLETQKLDLMAEISNLKLK 182
Cdd:COG5185   274 AESSKRLNENANNLIKQFENTKEKI-AEYTKSIDIKKATESLEEQLAAAEA--------EQELEESKRETETGIQNLTAE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 LtavekdrldyEDKFRDTEGLIQEIN-DLRLKVSEMDSERLqyEKKLKSTKDELASLKEQLEEKESEVKRlQEKLVCKMK 261
Cdd:COG5185   345 I----------EQGQESLTENLEAIKeEIENIVGEVELSKS--SEELDSFKDTIESTKESLDEIPQNQRG-YAQEILATL 411

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034581973 262 GEGVEIVDRDIEvqKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQG 317
Cdd:COG5185   412 EDTLKAADRQIE--ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRL 465
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 701-748 5.79e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.54  E-value: 5.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034581973 701 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 748
Cdd:cd09504     3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 134-300 6.01e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKdrldyedKFRDTEGLIQEINDLRLK 213
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQ 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 214 VSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRL---QEKLVCKMKgegveivDRDIEVQKMKKAVESLMAANEE 290
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLS-------EKQKELEQNNKKIKELEKQLNQ 292

                         170
                  ....*....|
gi 1034581973 291 KDRKIEDLRQ 300
Cdd:TIGR04523 293 LKSEISDLNN 302
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 42-346 6.05e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973   42 FMGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLendkesLVLQVS 121
Cdd:pfam02463  659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR------VQEAQD 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  122 VLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLD--LMAEISNLKLKLTAVEKDRLDYEDKFRD 199
Cdd:pfam02463  733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKteKLKVEEEKEEKLKAQEEELRALEEELKE 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  200 TEGLIQEINDLRLKVSEMDSERLQYEKKLK--STKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKM 277
Cdd:pfam02463  813 EAELLEEEQLLIEQEEKIKEEELEELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE 892

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034581973  278 KKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDGEYEELLNSSSISSLLDAQGFSDLEKS 346
Cdd:pfam02463  893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-308 7.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 104 ERLARLENDKESLVLQVSVLTDQVEAQgEKIRDLEFCLEEHREKV-NATEEMLQQELLSrtsLETQKLDLMAEISNLKLK 182
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLtGLTPEKLEKELEE---LEKAKEEIEEEISKITAR 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 183 LTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERL--QYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvckm 260
Cdd:PRK03918  414 IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKLRKELRELEKVL---- 489

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034581973 261 kgegveivDRDIEVQKMKKAVESLMAANEE-KDRKIEDLRQCLNRYKKM 308
Cdd:PRK03918  490 --------KKESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKL 530
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 104-300 8.62e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 8.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:TIGR00606  709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973  184 TAV---EKDRLDYEDKFRDTEGLIQEIN--DLRLKVSEMDSERLQYEKKLKSTKDELASLKEQLEEKESEVKRLQEKLvC 258
Cdd:TIGR00606  789 TDVtimERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT-N 867

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034581973  259 KMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 300
Cdd:TIGR00606  868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE 909
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
102-307 9.42e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 102 YQER-------LARLENDKESLVLQVSvltDQVEAQGEKirDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMA 174
Cdd:PRK02224  167 YRERasdarlgVERVLSDQRGSLDQLK---AQIEEKEEK--DLHERLNGLESELAELDEEIER-------YEEQREQARE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034581973 175 EISNLKLKLTAvekdrldYEDKFRDTEGLIQEINDLRLKVSEMDSERlqyekklKSTKDELASLKEQLEEKESEVKRLQE 254
Cdd:PRK02224  235 TRDEADEVLEE-------HEERREELETLEAEIEDLRETIAETERER-------EELAEEVRDLRERLEELEEERDDLLA 300

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034581973 255 KLvckmkgegvEIVDRDIEVqkMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 307
Cdd:PRK02224  301 EA---------GLDDADAEA--VEARREELEDRDEELRDRLEECRVAAQAHNE 342
 
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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