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Conserved domains on  [gi|1958769870|ref|XP_038963639|]
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liprin-beta-1 isoform X5 [Rattus norvegicus]

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 ...
 814-885 3.18e-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: 159.54  E-value: 3.18e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  814 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
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 ...
 729-791 9.60e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 9.60e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
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 ...
 655-718 3.95e-33

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: 121.95  E-value: 3.95e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 103-340 2.49e-11

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 68.17  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLVcKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKE 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ....*.
gi 1958769870  335 RKIEDL 340
Cdd:TIGR02169  931 EELSEI 936
 
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 ...
 814-885 3.18e-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: 159.54  E-value: 3.18e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  814 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
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 ...
 729-791 9.60e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 9.60e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
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 ...
 655-718 3.95e-33

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: 121.95  E-value: 3.95e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 731-791 2.80e-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: 79.62  E-value: 2.80e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 657-719 3.14e-14

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: 68.06  E-value: 3.14e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  657 KWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 719
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 655-719 9.88e-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: 61.16  E-value: 9.88e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870   655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 731-791 1.53e-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: 1.53e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-340 2.49e-11

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: 68.17  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLVcKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKE 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ....*.
gi 1958769870  335 RKIEDL 340
Cdd:TIGR02169  931 EELSEI 936
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 5.32e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 5.32e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-355 2.17e-10

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: 63.63  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  195 DRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWETLKDELASL 269
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  270 KEQLEEKECEVKRLQERLvcktkgegVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 349
Cdd:COG4942    163 AALRAELEAERAELEALL--------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234


                   ....*.
gi 1958769870  350 VQDPAA 355
Cdd:COG4942    235 EAAAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-332 4.16e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.93  E-value: 4.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTD---QVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNL 179
Cdd:PRK03918   192 EELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  180 KLKLTAVEKDRLD------YEDRFRDTEGLIQEINDlrlKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQ 253
Cdd:PRK03918   272 KKEIEELEEKVKElkelkeKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  254 RMEQKWETLKdELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILD----RDENIKRKLKEKNIEVQKMKKAVESLMAA 329
Cdd:PRK03918   349 ELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEelekAKEEIEEEISKITARIGELKKEIKELKKA 427


                   ...
gi 1958769870  330 NEE 332
Cdd:PRK03918   428 IEE 430
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-340 7.45e-10

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: 63.20  E-value: 7.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   54 DLRGLLEMMETDEKEgLRCQIPDSTAEMLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  211 RLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvgqMQYEKQRMEQKwetlKDELASLKEQLEEKECEVkrlqERLVCK 290
Cdd:pfam05483  334 EAQMEELNKAKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKN----EDQLKIITMELQKKSSEL----EEMTKF 399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  291 TKGEGVEIldrdENIKRKLKEKNI---EVQKMKKAVESLMAANEE-------KERKIEDL 340
Cdd:pfam05483  400 KNNKEVEL----EELKKILAEDEKlldEKKQFEKIAEELKGKEQElifllqaREKEIHDL 455
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-884 7.02e-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: 47.29  E-value: 7.02e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   815 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
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 ...
 814-885 3.18e-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: 159.54  E-value: 3.18e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  814 EVQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
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 ...
 729-791 9.60e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 9.60e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09566      1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 822-883 3.80e-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: 3.80e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  822 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 883
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 655-718 3.95e-33

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: 121.95  E-value: 3.95e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 818-885 2.31e-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: 2.31e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
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 ...
 734-791 3.27e-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: 84.89  E-value: 3.27e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769870  734 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09495      2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 731-791 2.80e-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: 79.62  E-value: 2.80e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
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 ...
 818-885 6.43e-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: 6.43e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09568      5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 663-718 1.77e-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: 68.79  E-value: 1.77e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  663 VCSWLAEQGLGS-YLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09494      2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 657-719 3.14e-14

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: 68.06  E-value: 3.14e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  657 KWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 719
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 734-788 7.67e-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: 63.80  E-value: 7.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  734 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 788
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 ...
 729-791 1.96e-12

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: 63.20  E-value: 1.96e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  729 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09567      1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 655-719 9.88e-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: 61.16  E-value: 9.88e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870   655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 731-791 1.53e-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: 1.53e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-340 2.49e-11

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: 68.17  E-value: 2.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLVcKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKE 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930


                   ....*.
gi 1958769870  335 RKIEDL 340
Cdd:TIGR02169  931 EELSEI 936
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 5.32e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 5.32e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-355 2.17e-10

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: 63.63  E-value: 2.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  195 DRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWETLKDELASL 269
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  270 KEQLEEKECEVKRLQERLvcktkgegVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 349
Cdd:COG4942    163 AALRAELEAERAELEALL--------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234


                   ....*.
gi 1958769870  350 VQDPAA 355
Cdd:COG4942    235 EAAAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-332 4.16e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.93  E-value: 4.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTD---QVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNL 179
Cdd:PRK03918   192 EELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  180 KLKLTAVEKDRLD------YEDRFRDTEGLIQEINDlrlKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQ 253
Cdd:PRK03918   272 KKEIEELEEKVKElkelkeKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  254 RMEQKWETLKdELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILD----RDENIKRKLKEKNIEVQKMKKAVESLMAA 329
Cdd:PRK03918   349 ELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEelekAKEEIEEEISKITARIGELKKEIKELKKA 427


                   ...
gi 1958769870  330 NEE 332
Cdd:PRK03918   428 IEE 430
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-340 7.45e-10

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: 63.20  E-value: 7.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   54 DLRGLLEMMETDEKEgLRCQIPDSTAEMLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  211 RLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvgqMQYEKQRMEQKwetlKDELASLKEQLEEKECEVkrlqERLVCK 290
Cdd:pfam05483  334 EAQMEELNKAKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKN----EDQLKIITMELQKKSSEL----EEMTKF 399

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  291 TKGEGVEIldrdENIKRKLKEKNI---EVQKMKKAVESLMAANEE-------KERKIEDL 340
Cdd:pfam05483  400 KNNKEVEL----EELKKILAEDEKlldEKKQFEKIAEELKGKEQElifllqaREKEIHDL 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-350 1.01e-09

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: 62.77  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQV-------SVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  176 ISNLKLKLTAVEKDRLDYEDRFRDT------------------EGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAK 237
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATerrledleeqieelsediESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  238 LSS----MKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDENIKRKLKEKN 313
Cdd:TIGR02168  892 LRSeleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  314 IEVQKMKKAVESL----MAANEE----KERK------IEDLRQCLSRYRKV 350
Cdd:TIGR02168  972 RRLKRLENKIKELgpvnLAAIEEyeelKERYdfltaqKEDLTEAKETLEEA 1022
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-349 1.05e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNE---MDSERLQYEKKLKSTKSLMAKLSSmKIKvgqmqyEKQRMEQK 258
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEE-EIN------GIEERIKE 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  259 WETLKDELASLKEQLEEKECEVKRLQERLvcKTKGEGVEILDRDENIKRKLKEKNIEvqKMKKAVESLMAANEEKERKIE 338
Cdd:PRK03918   333 LEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEIS 408

                          250
                   ....*....|.
gi 1958769870  339 DLRQCLSRYRK 349
Cdd:PRK03918   409 KITARIGELKK 419
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-340 1.12e-09

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: 62.35  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQV---EAQGEKIRDLEFCLEEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNL 179
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI---ERLKETIIKNNSEIKDL 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  180 KLKLTAVEkdrLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:TIGR04523  446 TNQDSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE----------EKKELEEKV 512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  260 ETLKDELASLKEQLEEKECEVKRLQERLvcKTKGEGVEILDRD---ENIKRKLKEKNIEVQKMKKAVESLMAANEEKERK 336
Cdd:TIGR04523  513 KDLTKKISSLKEKIEKLESEKKEKESKI--SDLEDELNKDDFElkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL 590


                   ....
gi 1958769870  337 IEDL 340
Cdd:TIGR04523  591 IDQK 594
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 662-717 1.14e-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: 54.94  E-value: 1.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769870  662 QVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 717
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-331 2.53e-09

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: 61.61  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---LNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  166 ETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSM 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  242 KIKVGQMQYEKQRME--QKWETLKDELASLKEQLEEKECEVKRLQERlvcktkgegveiLDRDENIKRKLKEKNIEVQKM 319
Cdd:TIGR02168  423 IEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELREE------------LEEAEQALDAAERELAQLQAR 490

                          250
                   ....*....|..
gi 1958769870  320 KKAVESLMAANE 331
Cdd:TIGR02168  491 LDSLERLQENLE 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-322 1.67e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQqELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQ-YEKQRMEQKWETL 262
Cdd:PRK03918   310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGLTPEKL 389

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  263 KDELASLKEQLEEKECEVKrlqerlvcktkgegvEILDRDENIKRKLKEKNIEVQKMKKA 322
Cdd:PRK03918   390 EKELEELEKAKEEIEEEIS---------------KITARIGELKKEIKELKKAIEELKKA 434
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-342 3.35e-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: 57.72  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEisnLKLKLTAVEK 188
Cdd:TIGR04523  300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  189 DRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWETLKDELAS 268
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----------EIERLKETIIKNNSEIKD 444

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  269 LKEQLEEKECEVKRL-QERLVCKTKGEGVEILDRdeNIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:TIGR04523  445 LTNQDSVKELIIKNLdNTRESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
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 ...
 730-792 5.56e-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: 50.55  E-value: 5.56e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  730 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 792
Cdd:cd09565      1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-366 6.85e-08

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: 54.55  E-value: 6.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  155 LQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKL---KST 231
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  232 KSLMAklssmkikvgqMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVcktkgegveilDRDENIKRKLKE 311
Cdd:COG1579     89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-----------ELEAELEEKKAE 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769870  312 KNIEVQKMKKAVESLMAANEEKERKI-EDLrqcLSRY---RKVQDPAALAQGQEGECEG 366
Cdd:COG1579    147 LDEELAELEAELEELEAEREELAAKIpPEL---LALYeriRKRKNGLAVVPVEGGACGG 202
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-340 1.60e-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: 55.84  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSR-TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFr 198
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRL- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  199 dtEGLIQEINDLRLKVNEMDSER-LQYEKKLKSTKSlmaklssmkikvgqmqyekqrmeqkwetlkdELASLKEQLEEKE 277
Cdd:TIGR02169  268 --EEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEA-------------------------------EIASLERSIAEKE 314

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  278 CEVKRLQERLVcKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDL 340
Cdd:TIGR02169  315 RELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-355 2.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  165 LETQKLELMAEISNLKLKLTAVEKDRLDYEDRfRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIK 244
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  245 VGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVE 324
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958769870  325 SLMAANEEKERKIEDLRQCLSRYRKVQDPAA 355
Cdd:COG4913    774 RIDALRARLNRAEEELERAMRAFNREWPAET 804
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 656-717 2.45e-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: 2.45e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  656 AKWTKEQVCSWL-AEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 717
Cdd:cd09564      2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-349 3.10e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  171 ELMAEISNLKLKLTAVEkdrlDYEDRFRDTEG----LIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVG 246
Cdd:PRK03918   173 EIKRRIERLEKFIKRTE----NIEELIKEKEKeleeVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  247 QMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQE-RLVCKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVES 325
Cdd:PRK03918   249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                          170       180
                   ....*....|....*....|....
gi 1958769870  326 LMAANEEKERKIEDLRQCLSRYRK 349
Cdd:PRK03918   329 RIKELEEKEERLEELKKKLKELEK 352
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 104-342 4.41e-07

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: 53.96  E-value: 4.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  104 ERLARLENDKESLVLQVSvltdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSletqklelmaEISNLKLKL 183
Cdd:pfam05483  394 EEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAVEKDRLDYedrFRDTEGLIQEINDLRLKVNEM--DSERLQYEKK--LKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:pfam05483  460 TAIKTSEEHY---LKEVEDLKTELEKEKLKNIELtaHCDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  260 ETLKDELASLKEQLEEKECEVKRLQERLVCKtkgegveiLDRDENIKRKLKEKNIEVQKMKKAVE----SLMAANEEKER 335
Cdd:pfam05483  537 ENLEEKEMNLRDELESVREEFIQKGDEVKCK--------LDKSEENARSIEYEVLKKEKQMKILEnkcnNLKKQIENKNK 608


                   ....*..
gi 1958769870  336 KIEDLRQ 342
Cdd:pfam05483  609 NIEELHQ 615
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-362 5.17e-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: 5.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  102 YQERLARLENDKESLV------------------------LQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQ 157
Cdd:COG1196    234 LRELEAELEELEAELEeleaeleeleaelaeleaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  158 ELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRL-KVNEMDSERLQYEKKLKSTKSLMA 236
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeAEAELAEAEEELEELAEELLEALR 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  237 KLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktkgegveiLDRDENIKRKLKEKNIEV 316
Cdd:COG1196    394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-----------EEAAEEEAELEEEEEALL 462

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1958769870  317 QKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQDPAALAQGQEG 362
Cdd:COG1196    463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 735-790 5.72e-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: 47.70  E-value: 5.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769870  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09506     10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-884 7.02e-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: 47.29  E-value: 7.02e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   815 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-349 7.55e-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: 53.52  E-value: 7.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  142 EEHREKLNATEEMLQQELLSRTSLETQ--KLELMAEisnlklkltAVEKDRlDYEDRFRDTEG--LIQEINDLRLKVNEM 217
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDILNELERQlkSLERQAE---------KAERYK-ELKAELRELELalLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  218 DSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL--VCKTKGEG 295
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEEL 321

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  296 VEILDRDEN-----------IKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 349
Cdd:TIGR02168  322 EAQLEELESkldelaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
152-351 8.68e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 8.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  152 EEMLQQELLSRTSLETQKLEL-MAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKkLKS 230
Cdd:COG4717     48 LERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQ 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  231 TKSLMAKLSSMKIKVGQMQYEKQRMEQKWEtlkdELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDENIKRKLK 310
Cdd:COG4717    127 LLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958769870  311 EKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQ 351
Cdd:COG4717    203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 156-342 9.76e-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: 51.08  E-value: 9.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  156 QQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKLKSTKSLM 235
Cdd:COG1579      6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK---TELEDLEKEIKRLELEIEEVEARIKKYEEQL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  236 AKLSSMKikvgqmQYEkqrmeqkweTLKDELASLKEQLEEKECEVKRLQERLvcktkgegveildrdENIKRKLKEKNIE 315
Cdd:COG1579     83 GNVRNNK------EYE---------ALQKEIESLKRRISDLEDEILELMERI---------------EELEEELAELEAE 132

                          170       180
                   ....*....|....*....|....*..
gi 1958769870  316 VQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:COG1579    133 LAELEAELEEKKAELDEELAELEAELE 159
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 735-787 1.34e-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: 46.15  E-value: 1.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 787
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-361 1.44e-06

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: 52.48  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  132 EKIRDLEFCLEEHREKLNATEEMLQQEL----LSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  208 ndLRLKVNEMDSERLQYEKK-------LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWETL 262
Cdd:pfam01576  417 --LQARLSESERQRAELAEKlsklqseLESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQL 494

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  263 KDELASLKEQLEEKEcEVKRLQERLVCKTKGEGVEildrdenIKRKLKEKNIEVQ-------KMKKAVESLMAANEEKER 335
Cdd:pfam01576  495 EDERNSLQEQLEEEE-EAKRNVERQLSTLQAQLSD-------MKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAA 566

                          250       260
                   ....*....|....*....|....*.
gi 1958769870  336 KIEDLRQCLSRYRKVQDPAALAQGQE 361
Cdd:pfam01576  567 AYDKLEKTKNRLQQELDDLLVDLDHQ 592
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
731-791 1.86e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.86e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 658-719 2.11e-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: 46.16  E-value: 2.11e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09505      5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-350 4.36e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  102 YQERLARLENDKESLvlqvsvlTDQVEAQGEKIRDLEFCLEEHREkLNATEEMLQQ--ELLSRTS-LETQKLELMA-EIS 177
Cdd:PRK03918   457 YTAELKRIEKELKEI-------EEKERKLRKELRELEKVLKKESE-LIKLKELAEQlkELEEKLKkYNLEELEKKAeEYE 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  178 NLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKL-----KSTKSLMAKLSSMK------IKVG 246
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyneyLELK 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  247 QMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEildRDENIKRKLKEKNIEVQKMKKAVESL 326
Cdd:PRK03918   609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEEL 685

                          250       260
                   ....*....|....*....|....
gi 1958769870  327 MAANEEKERKIEDLRQCLSRYRKV 350
Cdd:PRK03918   686 EKRREEIKKTLEKLKEELEEREKA 709
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
97-342 4.43e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.81  E-value: 4.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   97 GNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEI 176
Cdd:PRK02224   342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  177 SNLKLKLTAVEKDRLDYEDRFRDTEGLIQE------------------INDLRLKVNEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:PRK02224   422 DELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  239 SSMKikvgQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL-------------VCKTKGEGVEILDRDENI 305
Cdd:PRK02224   502 EDLV----EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAaeleaeaeekreaAAEAEEEAEEAREEVAEL 577

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1958769870  306 KRKLKEKNIEVQKMKKaVESLMAANEEKERKIEDLRQ 342
Cdd:PRK02224   578 NSKLAELKERIESLER-IRTLLAAIADAEDEIERLRE 613
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
102-361 4.98e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.52  E-value: 4.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:COG1340     13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDL--RLKVNEMDSERlqyEKKLkstkslMAKLSSM--KIKVGQMQYEKQRmeq 257
Cdd:COG1340     93 ELDELRKELAELNKAGGSIDKLRKEIERLewRQQTEVLSPEE---EKEL------VEKIKELekELEKAKKALEKNE--- 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  258 KWETLKDELASLKEQLEEKECEVKRLQERlVCKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKI 337
Cdd:COG1340    161 KLKELRAELKELRKEAEEIHKKIKELAEE-AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239

                          250       260
                   ....*....|....*....|....
gi 1958769870  338 EDLRQCLSRYRKVQDPAALAQGQE 361
Cdd:COG1340    240 RELRKELKKLRKKQRALKREKEKE 263
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-349 5.38e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   90 MTNGHLPGNGDV-----YQERLARLENDKESLVLQVSVLTDQVEAQ----GEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:TIGR02169  655 MTGGSRAPRGGIlfsrsEPAELQRLRERLEGLKRELSSLQSELRRIenrlDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  161 SRTSLEtqklELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSE---------RLQYEKKLKST 231
Cdd:TIGR02169  735 LKERLE----ELEEDLSSLEQEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARlshsripeiQAELSKLEEEV 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  232 KSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVkrlqerlvcktkgegveildrdENIKRKLKE 311
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI----------------------ENLNGKKEE 865

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958769870  312 KNIEVqkmkkaveslmaanEEKERKIEDLRQCLSRYRK 349
Cdd:TIGR02169  866 LEEEL--------------EELEAALRDLESRLGDLKK 889
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-365 5.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDRfrdTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWETL 262
Cdd:COG1196    388 LLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE----------ALEEAAEEEAEL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  263 KDELASLKEQLEEKECEVKRLQERLVcktkgegVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIE---- 338
Cdd:COG1196    455 EEEEEALLELLAELLEEAALLEAALA-------ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgava 527

                          250       260
                   ....*....|....*....|....*..
gi 1958769870  339 DLRQCLSRYRKVQDPAALAQGQEGECE 365
Cdd:COG1196    528 VLIGVEAAYEAALEAALAAALQNIVVE 554
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-361 5.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 5.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  104 ERLARLEN--DKESLVLQVSVLTDQVEAQGEK-----IRDLEFCLEEHRE------KLNATEEMLQQELLSRTSLETQKL 170
Cdd:PRK03918   480 KELRELEKvlKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKlkekliKLKGEIKSLKKELEKLEELKKKLA 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  171 ELMAEISNLKLKLTAVEK--DRLDYEDrFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQM 248
Cdd:PRK03918   560 ELEKKLDELEEELAELLKelEELGFES-VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  249 QYEKQRMEQKWETLK-----DELASLKEQLEEKECEVKRLQERLvcktkgEGVEilDRDENIKR---KLKEKNIEVQKMK 320
Cdd:PRK03918   639 EKRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAEL------EELE--KRREEIKKtleKLKEELEEREKAK 710

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958769870  321 KAVESLMAANEekerKIEDLRQCLSRYRKVQDPAALAQGQE 361
Cdd:PRK03918   711 KELEKLEKALE----RVEELREKVKKYKALLKERALSKVGE 747
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 ...
 655-719 7.17e-06

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: 44.86  E-value: 7.17e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  655 FAKWTKEQVCSWLaEQGLGS---YLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09562      1 FALWNGPTVVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 163-345 8.78e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  163 TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSlmaklssmk 242
Cdd:TIGR04523  169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ--------- 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  243 iKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEG---VEILD----RDENIKRKLKEKNIE 315
Cdd:TIGR04523  240 -EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDlnnqKEQDWNKELKSELKN 318

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958769870  316 VQKMKKAVESLMAANEEK----ERKIEDLRQCLS 345
Cdd:TIGR04523  319 QEKKLEEIQNQISQNNKIisqlNEQISQLKKELT 352
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 654-719 8.97e-06

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 44.33  E-value: 8.97e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  654 PFAKWTKEQVCSWLAEQGLGSYLSS-GKHWImSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09507      1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 107-340 1.17e-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: 49.73  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  107 ARLENDKESLVLQVSVLTDQ---VEAQGEKIRDLEFCLEEHREKLNATEEMLQQeLLSRTSLETQKLE-LMAEISNLK-- 180
Cdd:pfam15921  468 AQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITK-LRSRVDLKLQELQhLKNEGDHLRnv 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  181 ------LKLTAVEKD------RLDYEDRFR------DTEGLIQ--------EINDLRLKVNEMdserlqyeKKLKSTKSl 234
Cdd:pfam15921  547 qteceaLKLQMAEKDkvieilRQQIENMTQlvgqhgRTAGAMQvekaqlekEINDRRLELQEF--------KILKDKKD- 617

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  235 mAKLSSMKIKVGQMQYEKQRM----EQKWETLKDelasLKEQLEEKECEVKRLQERLvcKTKGEGVEILDRdeNIKRKLK 310
Cdd:pfam15921  618 -AKIRELEARVSDLELEKVKLvnagSERLRAVKD----IKQERDQLLNEVKTSRNEL--NSLSEDYEVLKR--NFRNKSE 688

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958769870  311 EKNIEVQKMKKAVESLMAANEEKERKIEDL 340
Cdd:pfam15921  689 EMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
PRK01156 PRK01156
chromosome segregation protein; Provisional
 109-340 1.67e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.13  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  109 LENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEE---MLQQELLSRTSLETQKLELMAEISNLKLKLTA 185
Cdd:PRK01156   188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  186 VEKDRLDYE------------------DRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQ 247
Cdd:PRK01156   268 ELEKNNYYKeleerhmkiindpvyknrNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  248 M-QYEKQRM-----EQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGV---EILDRDENIKRKLKEKNIEVQK 318
Cdd:PRK01156   348 YdDLNNQILelegyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIdpdAIKKELNEINVKLQDISSKVSS 427

                          250       260
                   ....*....|....*....|..
gi 1958769870  319 MKKAVESLMAANEEKERKIEDL 340
Cdd:PRK01156   428 LNQRIRALRENLDELSRNMEML 449
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-287 2.17e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEML---------QQELLS-------RTSLE 166
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaeieeRREELGeraralyRSGGS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  167 TQKLELMAEISNLKlklTAVekDRLDYEDRFRDTEG-LIQEINDLRLKVNEmdsERLQYEKKLKSTKSLMAKLSSMKikv 245
Cdd:COG3883    102 VSYLDVLLGSESFS---DFL--DRLSALSKIADADAdLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAK--- 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958769870  246 GQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG3883    171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-350 2.42e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  141 LEEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDlRLKVNEMDSE 220
Cdd:TIGR04523  223 LKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  221 RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEvkrlqerlvcktkgegveild 300
Cdd:TIGR04523  299 DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE--------------------- 357

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958769870  301 rDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKV 350
Cdd:TIGR04523  358 -NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
PTZ00121 PTZ00121
MAEBL; Provisional
 142-342 2.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  142 EEHR--EKLNATEEMLQQELLsRTSLETQKLELMAEISNLKL--KLTAVEKDRLDYEDR---FRDTEGL-------IQEI 207
Cdd:PTZ00121  1519 EEAKkaDEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKnmaLRKAEEAkkaeearIEEV 1597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  208 NDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLK---DELASLKEQLEEKECEVKRLQ 284
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKAEEDKKKA 1677

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  285 ERL--VCKTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:PTZ00121  1678 EEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 103-365 3.34e-05

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: 47.89  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ------QELLSRTSLETQKLELMAEI 176
Cdd:pfam10174  365 TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkervKSLQTDSSNTDTALTTLEEA 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  177 SNLKLKLTAVEKDRLDYEDRFR--DTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKL-SSMKIKVGQMQYEKQ 253
Cdd:pfam10174  445 LSEKERIIERLKEQREREDRERleELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLaSSGLKKDSKLKSLEI 524

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  254 RMEQKwetlKDELASLKEQLeekecevKRLQERLVCKTKGEgvEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEE- 332
Cdd:pfam10174  525 AVEQK----KEECSKLENQL-------KKAHNAEEAVRTNP--EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREv 591

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958769870  333 ------KERKIEDLRQCLSRYRKVQdPAALAQGQEGECE 365
Cdd:pfam10174  592 enekndKDKKIAELESLTLRQMKEQ-NKKVANIKHGQQE 629
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 87-367 3.63e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   87 QNQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEA-QGEKIRDLEFCLEEHREKLNA------------TE- 152
Cdd:pfam15921  207 HDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQliseheveitglTEk 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  153 ---------------EMLQQELLSRTSLETQKL-ELMAEISNLKLKLTavEKDRLdYEDRFRDTEGLIQEINDlrlKVNE 216
Cdd:pfam15921  287 assarsqansiqsqlEIIQEQARNQNSMYMRQLsDLESTVSQLRSELR--EAKRM-YEDKIEELEKQLVLANS---ELTE 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  217 MDSERLQYEKKLKSTKSLMAKL-SSMKIKVGQMQYEKQRMEQKWEtlKD-----ELASLKEQLEEKECEVKRLQ------ 284
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQKLlADLHKREKELSLEKEQNKRLWD--RDtgnsiTIDHLRRELDDRNMEVQRLEallkam 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  285 --------ERLVCKTKGEGVEI---------LDRDENIKRKLKE----KNIEVQKMKKAVESLMAANEEKERKIEDLRQC 343
Cdd:pfam15921  439 ksecqgqmERQMAAIQGKNESLekvssltaqLESTKEMLRKVVEeltaKKMTLESSERTVSDLTASLQEKERAIEATNAE 518

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1958769870  344 LSRYR-----KVQDPAALA------QGQEGECEGL 367
Cdd:pfam15921  519 ITKLRsrvdlKLQELQHLKnegdhlRNVQTECEAL 553
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 732-790 4.39e-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: 4.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  732 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09530      1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-358 4.42e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  100 DVYQERLaRLENDKESLVLQVSVL-TDQVEAQ--GEKIRD--LEFCLEEHREKLNATEEMLQQELlsrTSLETQKLELMA 174
Cdd:COG3206    121 ERLRKNL-TVEPVKGSNVIEISYTsPDPELAAavANALAEayLEQNLELRREEARKALEFLEEQL---PELRKELEEAEA 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  175 EISNLKLK--LTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmQYEK 252
Cdd:COG3206    197 ALEEFRQKngLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--------SPVI 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  253 QRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktkgEGVEILDRDEnIKRKLKEKNIEVQKMKKAVESLMAANEE 332
Cdd:COG3206    266 QQLRAQLAELEAELAELSARYTPNHPDVIALRAQI------AALRAQLQQE-AQRILASLEAELEALQAREASLQAQLAQ 338

                          250       260
                   ....*....|....*....|....*.
gi 1958769870  333 KERKIEDLRQCLSRYRKVQDPAALAQ 358
Cdd:COG3206    339 LEARLAELPELEAELRRLEREVEVAR 364
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-287 4.93e-05

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: 46.68  E-value: 4.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEE---MLQQELLS--------RTSLETQKLE 171
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAElekeiaelRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  172 L---------MAEISNLKLKLTAVEKD----RLDYEDRFrdTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:COG4942    106 LaellralyrLGRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769870  239 SSMKIKVGQMQYEKQRMEQKwetLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG4942    184 EEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 658-719 5.32e-05

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: 42.29  E-value: 5.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09501      4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 103-381 5.68e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.27  E-value: 5.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  168 QklelMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMaklssmkikvgQ 247
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH-----------T 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  248 MQYEKQRMEQKWETLKDELASLKEQLEEKECEVKR---LQERLVCKTKGEGVEIldRDENIKRKLKEKNIEVQKMKKAVE 324
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQELQQ--RYAELCAAAITCTAQCEKLEKIHL 461

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  325 SLMA-ANEEKERKIEDLRQCLSRY-RKVQDPAALAQGQEGE----CEGLFHSSSISTLLDAQG 381
Cdd:TIGR00618  462 QESAqSLKEREQQLQTKEQIHLQEtRKKAVVLARLLELQEEpcplCGSCIHPNPARQDIDNPG 524
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-342 1.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  147 KLNATEEMLQ------QELLSR-TSLETQK------LELMAEISNLKLKLTAVEKDRLD-----YEDRFRDTEGLIQEIN 208
Cdd:COG1196    180 KLEATEENLErledilGELERQlEPLERQAekaeryRELKEELKELEAELLLLKLRELEaeleeLEAELEELEAELEELE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  209 -DLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG1196    260 aELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958769870  288 vcktkgegVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:COG1196    340 --------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 106-350 1.34e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  106 LARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQ--ELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:TIGR04523  498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQ 577

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmqyekqrmEQKWETLK 263
Cdd:TIGR04523  578 KSLKKKQEEKQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI----------KSKKNKLK 644

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  264 DELASLKEQLEekecEVKRLQERLVCKTKGEGVEILDRDENIKRKLKEKNIEVqkmKKAVESLMAAN-----EEKERKIE 338
Cdd:TIGR04523  645 QEVKQIKETIK----EIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHY---KKYITRMIRIKdlpklEEKYKEIE 717

                          250
                   ....*....|..
gi 1958769870  339 DLRQCLSRYRKV 350
Cdd:TIGR04523  718 KELKKLDEFSKE 729
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
658-719 1.60e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.72  E-value: 1.60e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  658 WTKEQVCSWLAEQGLGSYLSS-GKHWIMSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
104-348 1.66e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKlnateemlqqellsRTSLETqkleLMAEISNLKLKL 183
Cdd:PRK02224   206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER--------------REELET----LEAEIEDLRETI 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAVEKDRLDYEDRFRD----TEGLIQEINDLRlkvNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:PRK02224   268 AETEREREELAEEVRDlrerLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  260 ETLKDELASLKEQLEEKECEVKRLQERLvcktKGEGVEILDRDEnikrKLKEKNIEVQKMKKAVESLMAANEEKERKIED 339
Cdd:PRK02224   345 ESLREDADDLEERAEELREEAAELESEL----EEAREAVEDRRE----EIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416


                   ....*....
gi 1958769870  340 LRQCLSRYR 348
Cdd:PRK02224   417 LREERDELR 425
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-308 1.94e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  133 KIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDR------FRDTEGLIQE 206
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  207 INDLRLKVNEMDSERLQyekklkstksLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQER 286
Cdd:COG1579     98 IESLKRRISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167

                          170       180
                   ....*....|....*....|..
gi 1958769870  287 LVcktKGEGVEILDRDENIKRK 308
Cdd:COG1579    168 LA---AKIPPELLALYERIRKR 186
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 2.34e-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: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ 156
Cdd:pfam01519   26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 218-349 2.41e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  218 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL-----V 288
Cdd:COG3883     15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarA 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  289 CKTKGEGV-------------EILDRDENIKR---KLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 349
Cdd:COG3883     95 LYRSGGSVsyldvllgsesfsDFLDRLSALSKiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
PRK12704 PRK12704
phosphodiesterase; Provisional
 232-342 2.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  232 KSLMAKLSSMKIKVGQM--QYEKQRMEQKWETL---KDELASLKEQLE----EKECEVKRLQERLvcktkgegveiLDRD 302
Cdd:PRK12704    27 KIAEAKIKEAEEEAKRIleEAKKEAEAIKKEALleaKEEIHKLRNEFEkelrERRNELQKLEKRL-----------LQKE 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958769870  303 ENIKRK---LKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:PRK12704    96 ENLDRKlelLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 112-342 3.21e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 3.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  112 DKESLVL----QVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEML----QQELLSRTSLE-TQKLELM--------- 173
Cdd:pfam10174  493 EKESSLIdlkeHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevaryke 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  174 ------AEISNLKLKLTAVEKDRLDYEDRFRDTEGLI--------QEINDLRLKVNEMDSERLQ-YEKKLKSTKSLMAKL 238
Cdd:pfam10174  573 esgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNS 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  239 SSMKIKVGQMQYEKQRmeQKWETLKDELASLKEQLEEKECEV--------KRLQERLVCKTKGEGVEILDRDENIKrkLK 310
Cdd:pfam10174  653 QQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDGHLtnlraerrKQLEEILEMKQEALLAAISEKDANIA--LL 728

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1958769870  311 EknIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:pfam10174  729 E--LSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 735-792 3.55e-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: 3.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769870  735 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 792
Cdd:cd09547      6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 732-791 4.90e-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: 4.90e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  732 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09552      6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-228 5.32e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEM------------LQQEL----LSRTSLE 166
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  167 TQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEG-LIQEINDLRLKVNEMDSERLQYEKKL 228
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAELEELEAEREELAAKI 172
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 42-342 5.51e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   42 FMGSLRALHLVEDLRGLLEMMETDEKEglrcqipdSTAEMLIEWLQNQMTNGHLPGNGDVYQERLARLENDKESLVLQ-- 119
Cdd:pfam02463  659 AEKSEVKASLSELTKELLEIQELQEKA--------ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQea 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKL--ELMAEISNLKLKLTAVEKDRLDYEDRF 197
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREktEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  198 RDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWET--LKDELASLKEQLEE 275
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLkeEELEEQKLKDELES 890

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  276 KECEVKR-LQERLVCKTKGEGVEILDR----DENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:pfam02463  891 KEEKEKEeKKELEEESQKLNLLEEKENeieeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-387 5.58e-04

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: 44.01  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  109 LENDKESLVLQVSVLTdQVEAQGE-KIRDLEFCLEEHREKLNATEEmLQQELLSRTSLETQKLE-LMAEISNLKLKLTAV 186
Cdd:pfam01576  382 LESENAELQAELRTLQ-QAKQDSEhKRKKLEGQLQELQARLSESER-QRAELAEKLSKLQSELEsVSSLLNEAEGKNIKL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  187 EKDRLDYEDRFRDTEGLIQEINDLRL----KVNEMDSERLQYEKKL-----------KSTKSLMAKLSSMKIKVGQMQYE 251
Cdd:pfam01576  460 SKDVSSLESQLQDTQELLQEETRQKLnlstRLRQLEDERNSLQEQLeeeeeakrnveRQLSTLQAQLSDMKKKLEEDAGT 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  252 KQRMEQKWETLKDELASLKEQLEEKECEVKRLQerlvcKTKgegveildrdENIKRKLKEKNIEVQKMKKAVESLmaanE 331
Cdd:pfam01576  540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-----KTK----------NRLQQELDDLLVDLDHQRQLVSNL----E 600

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  332 EKERKIEDL----RQCLSRYRKVQDPAAlAQGQEGECEGLFHSSSISTLLDAQgfSDLER 387
Cdd:pfam01576  601 KKQKKFDQMlaeeKAISARYAEERDRAE-AEAREKETRALSLARALEEALEAK--EELER 657
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-286 6.25e-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: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKLNATEEMLQQELLSRTSLETQKLElmAEISNLKLK 182
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIRGNGGDRLEQLE--REIERLERE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDRfrdtegliqeINDLRLKVnemDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWETL 262
Cdd:COG4913    354 LEERERRRARLEAL----------LAALGLPL---PASAEEFAALRAEAAALLEALEE----------ELEALEEALAEA 410

                          170       180
                   ....*....|....*....|....
gi 1958769870  263 KDELASLKEQLEEKECEVKRLQER 286
Cdd:COG4913    411 EAALRDLRRELRELEAEIASLERR 434
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 103-314 6.33e-04

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: 43.89  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGE-------KIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLElmae 175
Cdd:TIGR01612 1536 KNKFAKTKKDSEIIIKEIKDAHKKFILEAEkseqkikEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLK---- 1611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  176 ISNLKLKLT-------AVEKDRLDYEDRFRDTE--GLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVG 246
Cdd:TIGR01612 1612 ISDIKKKINdclketeSIEKKISSFSIDSQDTElkENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVD 1691

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  247 QMQ--YEKQRMEQKWETLKDElaslKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDENIKRKLKEKNI 314
Cdd:TIGR01612 1692 QHKknYEIGIIEKIKEIAIAN----KEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGD 1757
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-286 7.52e-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: 43.52  E-value: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellsrtsLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-------LESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLDYEDrfrDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvGQMQYEKQRMEQKWETL 262
Cdd:TIGR02169  898 LRELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL----EDVQAELQRVEEEIRAL 970

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958769870  263 --------------KDELASLKEQLEEKECEVKRLQER 286
Cdd:TIGR02169  971 epvnmlaiqeyeevLKRLDELKEKRAKLEEERKAILER 1008
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 170-340 9.18e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 9.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  170 LELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLR-------LKVNEMDSERLQYEKKLKSTKSLMAKLSSMK 242
Cdd:pfam13851   22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTeplqkaqEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  243 IKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKR--------LQERLvcKTKGEGVEIldRDENIKRKLKEKNI 314
Cdd:pfam13851   99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAANL 174

                          170       180
                   ....*....|....*....|....*.
gi 1958769870  315 EVQKMKKAVESLMAANEEKERKIEDL 340
Cdd:pfam13851  175 DPDALQAVTEKLEDVLESKNQLIKDL 200
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 658-714 1.08e-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: 38.47  E-value: 1.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  658 WTKEQVCSWLAEQ-GLGSYLSSGKHWIMSGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 714
Cdd:cd09504      5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 104-339 1.13e-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: 43.11  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:TIGR00606  709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAV---EKDRLDYEDRFRDTEGLIQEIN--DLRLKVNEMDSERLQYEKKLKST---------------------KSLMAK 237
Cdd:TIGR00606  789 TDVtimERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVvskielnrkliqdqqeqiqhlKSKTNE 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  238 LSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVcKTKGEGVEILDRDENIKRKLKEKnieVQ 317
Cdd:TIGR00606  869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE-KDQQEKEELISSKETSNKKAQDK---VN 944

                          250       260
                   ....*....|....*....|..
gi 1958769870  318 KMKKAVESLMAANEEKERKIED 339
Cdd:TIGR00606  945 DIKEKVKNIHGYMKDIENKIQD 966
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 732-790 1.26e-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: 37.98  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09488      2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
206-342 1.36e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  206 EINDLRLKVNEMDSERL-QYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQ 284
Cdd:COG4372     14 SLFGLRPKTGILIAALSeQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  285 ERLVC------KTKGEGVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:COG4372     94 AELAQaqeeleSLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 654-710 1.39e-03

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 38.02  E-value: 1.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  654 PFAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLeKELGI-----KHSLHRK 710
Cdd:cd09512      3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
184-287 1.57e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  184 TAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 259
Cdd:COG2433    402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467

                           90       100
                   ....*....|....*....|....*...
gi 1958769870  260 ETLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG2433    468 SRLDREIERLERELEEERERIEELKRKL 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-350 1.60e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  192 DYEDRFRDTEGLIQEINDLR------LKVNEMDSERL-----QYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQkwe 260
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIerlekfIKRTENIEELIkekekELEEVLREINEISSELPELREELEKLEKEVKELEE--- 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  261 tLKDELASLKEQLEEKECEVKRLQERLVcktkgegvEILDRDEnikrKLKEKNIEVQKMKKAVESLmaanEEKERKIEDL 340
Cdd:PRK03918   236 -LKEEIEELEKELESLEGSKRKLEEKIR--------ELEERIE----ELKKEIEELEEKVKELKEL----KEKAEEYIKL 298

                          170
                   ....*....|
gi 1958769870  341 RQCLSRYRKV 350
Cdd:PRK03918   299 SEFYEEYLDE 308
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 103-337 1.63e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.42  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMlqQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:pfam05557   51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA--REVISCLKNELSELRRQIQRAELELQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  183 LTAVEKDRLdyedrfrdtegliQEINDL-RLKVNEMDSERLQYEKKLKStkslmakLSSMKIKVGQMQYEKQRMEQKWET 261
Cdd:pfam05557  129 STNSELEEL-------------QERLDLlKAKASEAEQLRQNLEKQQSS-------LAEAEQRIKELEFEIQSQEQDSEI 188

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  262 LKDELASLkEQLEEKECEVKRLQERLVC-KTKGEGVEILDRD-ENIKRKLKekniEVQKMKKAVESLMAANEEKERKI 337
Cdd:pfam05557  189 VKNSKSEL-ARIPELEKELERLREHNKHlNENIENKLLLKEEvEDLKRKLE----REEKYREEAATLELEKEKLEQEL 261
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 43-370 1.70e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   43 MGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAEmliewLQNQMTNGHLPGngdVYQERLARLENDkeslVLQVSV 122
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPG---PLTRRMQRGEQT----YAQLET 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  123 LTDQVEAQGEKIRdlefcleEHREKLNATEEMLQQELLSRTSLETqklELMAEISNLkLKLTAVEKDRLDYEDRFRDTEG 202
Cdd:TIGR00618  543 SEEDVYHQLTSER-------KQRASLKEQMQEIQQSFSILTQCDN---RSKEDIPNL-QNITVRLQDLTEKLSEAEDMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  203 LIQEINDLRLKVNEMDSERLQYEK-------KLKSTKSLMA--------KLSSMKIKVGQMQY--EKQRMEQKWETLKDE 265
Cdd:TIGR00618  612 CEQHALLRKLQPEQDLQDVRLHLQqcsqelaLKLTALHALQltltqervREHALSIRVLPKELlaSRQLALQKMQSEKEQ 691

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  266 LASLKEQL----------EEKECEVKRLQERLVCKTKGEGVEILDRDENIKRKLKEknievqKMKKAVESLMAANEEKER 335
Cdd:TIGR00618  692 LTYWKEMLaqcqtllrelETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE------LMHQARTVLKARTEAHFN 765

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1958769870  336 KIEDLRQCLSRYRKVQDPAALAQGQEGECEGLFHS 370
Cdd:TIGR00618  766 NNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL 800
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
125-340 1.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  125 DQVEAQGEKIRDLEFCLEEHREKLNAT-EEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGL 203
Cdd:COG4372      2 DRLGEKVGKARLSLFGLRPKTGILIAAlSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  204 IQEIN--------DLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEE 275
Cdd:COG4372     82 LEELNeqlqaaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  276 KECEVKRLQERLVCKTKGEGVEILDR--DENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDL 340
Cdd:COG4372    162 LQEELAALEQELQALSEAEAEQALDEllKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 164-337 2.03e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  164 SLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEmdserlQYEKKLKSTKSLMAKLssmkI 243
Cdd:PRK00409   524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEK------EAQQAIKEAKKEADEI----I 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  244 KVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDEN--IKRKLKEKNIEVQ---- 317
Cdd:PRK00409   591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKgeVLSIPDDKEAIVQagim 670

                          170       180
                   ....*....|....*....|...
gi 1958769870  318 KMK---KAVESLMAANEEKERKI 337
Cdd:PRK00409   671 KMKvplSDLEKIQKPKKKKKKKP 693
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 814-866 2.28e-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: 2.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  814 EVQQWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 866
Cdd:cd09504      1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 108-358 2.30e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  108 RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVE 187
Cdd:pfam01576  205 ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  188 KDRLDYEDRFRDtegLIQEINDLRLKV----------NEMDSERLQYEKKLK-----STKSLMAKLSSMKIKVGQ----- 247
Cdd:pfam01576  285 AARNKAEKQRRD---LGEELEALKTELedtldttaaqQELRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQaleel 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  248 -------------MQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktkgegVEILDRDENIKRKLKEKNI 314
Cdd:pfam01576  362 teqleqakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQL--------QELQARLSESERQRAELAE 433

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1958769870  315 EVQKMKKAVESLMAANEEKERK-IEDLRQCLSRYRKVQDPAALAQ 358
Cdd:pfam01576  434 KLSKLQSELESVSSLLNEAEGKnIKLSKDVSSLESQLQDTQELLQ 478
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 125-360 2.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  125 DQVEAQGEKIRDLEFCLEEHREKLNAteemLQQELlsrTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLI 204
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDA----LQAEL---EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  205 QEindlRLKVNEMDSERLQYEKKLKSTKSLmaklSSMkikVGQMQYEKQRMEQKWETLkDELASLKEQLEEKECEVKRLQ 284
Cdd:COG3883     89 GE----RARALYRSGGSVSYLDVLLGSESF----SDF---LDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769870  285 ERLVCKTKgegvEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQDPAALAQGQ 360
Cdd:COG3883    157 AELEALKA----ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 658-702 2.46e-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: 37.34  E-value: 2.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958769870  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQ---QDLEKELG 702
Cdd:cd09526      4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
PRK01156 PRK01156
chromosome segregation protein; Provisional
 114-356 2.54e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  114 ESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellsRTSLETQKLELMAEISNLKLKLTAVEKDRLDY 193
Cdd:PRK01156   162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQ----IADDEKSHSITLKEIERLSIEYNNAMDDYNNL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  194 EDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLssMKIKVGQMQYEKQRMEQKWeTLKDELASLKEQL 273
Cdd:PRK01156   238 KSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH--MKIINDPVYKNRNYINDYF-KYKNDIENKKQIL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  274 EEKECEVKRLQERLvckTKGEGVEiLDRDENIKRK------------LKEKNIEVQKMKKAVESLMAANEEKERKIEDLR 341
Cdd:PRK01156   315 SNIDAEINKYHAII---KKLSVLQ-KDYNDYIKKKsryddlnnqileLEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS 390

                          250
                   ....*....|....*..
gi 1958769870  342 QCLSRYRKVQ--DPAAL 356
Cdd:PRK01156   391 AFISEILKIQeiDPDAI 407
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 212-321 2.58e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  212 LKVNEM----DSERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWETLKDELASLKEQLEEK--------ECE 279
Cdd:PRK00409   516 EKLNELiaslEELERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKE 585

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958769870  280 VKRLQERLVCKTKGEGVEILDRD-ENIKRKLKEKNIEVQKMKK 321
Cdd:PRK00409   586 ADEIIKELRQLQKGGYASVKAHElIEARKRLNKANEKKEKKKK 628
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-288 2.69e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   84 EWLQNQMtNGHLPGNGDVYQERLA---RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:pfam07888   30 ELLQNRL-EECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  161 SRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKV----NEMDSERLQYEKKLKST----K 232
Cdd:pfam07888  109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEEAERKQLQAKLQQTeeelR 188

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769870  233 SLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKEC---EVKRLQERLV 288
Cdd:pfam07888  189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAlleELRSLQERLN 247
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 234-336 2.71e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  234 LMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQER----LVCKTKGEGVEILdRDENIKRKL 309
Cdd:PRK00409   521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaqqAIKEAKKEADEII-KELRQLQKG 599

                           90       100
                   ....*....|....*....|....*..
gi 1958769870  310 KEKNIEVQKMKKAVESLMAANEEKERK 336
Cdd:PRK00409   600 GYASVKAHELIEARKRLNKANEKKEKK 626
SAM_BAR cd09513
SAM domain of BAR subfamily; SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis ...
 656-717 2.92e-03

SAM domain of BAR subfamily; SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis Regulator) subfamily is a protein-protein interaction domain. In addition to the SAM domain, this type of regulator has a RING finger domain. Proteins of this subfamily are involved in the apoptosis signal network. Their overexpression in human neuronal cells significantly protects cells from a broad range of cell death stimuli. SAM domain can interact with Caspase8, Bcl-2 and Bcl-X resulting in suppression of Bax-induced cell death.


Pssm-ID: 188912  Cd Length: 71  Bit Score: 37.47  E-value: 2.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  656 AKWTKEQVCSWLAEqgLGSYLSSGKHWIMS----GQTLLQASQQDLEKE-LGIKHSLHRKKLQLALQ 717
Cdd:cd09513      2 SKWTPEEVVLWLEQ--LGPWASLYRERFLSenvnGRLLLTLTEEELSKPpFNIENSLHRRAILTELE 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 146-360 3.42e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  146 EKLNATEEMLQ--QELLSRTSLETQKLE-----LMAEISNLKLKLTA-------VEKDRLDYEDRFRDTEGLIQEInDLR 211
Cdd:pfam01576    5 EEMQAKEEELQkvKERQQKAESELKELEkkhqqLCEEKNALQEQLQAetelcaeAEEMRARLAARKQELEEILHEL-ESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  212 LKVNEMDSERLQYEKKLKST--KSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVC 289
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769870  290 KTKGEGVEildrdenikrklKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRY-RKVQDPAALAQGQ 360
Cdd:pfam01576  164 FTSNLAEE------------EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAkRKLEGESTDLQEQ 223
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 656-719 3.68e-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: 36.84  E-value: 3.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769870  656 AKWTKEQVCSWLAEQGLGSY--LSSGKHWImSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09515      2 HEWTCEDVAKWLKKEGFSKYvdLLCNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 735-791 3.76e-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: 3.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09505     10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 162-289 3.84e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.36  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  162 RTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRfrdTEGLIQEindlrLKVNEMDSERLqyEKKLKSTKSLMAKLSSM 241
Cdd:pfam20492    1 REEAEREKQELEERLKQYEEETKKAQEELEESEET---AEELEEE-----RRQAEEEAERL--EQKRQEAEEEKERLEES 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958769870  242 KIKvgqMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVC 289
Cdd:pfam20492   71 AEM---EAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEE 115
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 111-342 4.62e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.56  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  111 NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLE------------------- 171
Cdd:pfam15905   73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLEltrvnellkakfsedgtqk 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  172 ----LMAEISNLKLKLTAVEKDRLDyedRFRDTEGLIQEIN-DL--------RLKVNEMDSERLQYEKKLKSTKSL--MA 236
Cdd:pfam15905  153 kmssLSMELMKLRNKLEAKMKEVMA---KQEGMEGKLQVTQkNLehskgkvaQLEEKLVSTEKEKIEEKSETEKLLeyIT 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  237 KLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKgegvEILDRDENIKRKLKEK---- 312
Cdd:pfam15905  230 ELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK----LLESEKEELLREYEEKeqtl 305

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958769870  313 NIEVQKMKKAVESlmaaneeKERKIEDLRQ 342
Cdd:pfam15905  306 NAELEELKEKLTL-------EEQEHQKLQQ 328
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 656-704 4.68e-03

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 36.50  E-value: 4.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  656 AKWTKEQVCSWLaeQGLGS----YLSSGKHWIMSGQTLLQASQQDLEkELGIK 704
Cdd:cd09511      2 AKWSPKQVTDWL--KGLDDclqqYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
Filament pfam00038
Intermediate filament protein;
125-342 4.69e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.29  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  125 DQVEAQGEKIRDLEFCLEEHREKLNAT----EEMLQQEL--LSRT--SLETQKLELMAEISNLKLkltAVEKDRLDYEDR 196
Cdd:pfam00038   18 DKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  197 FRDTEGLIQEINDLRLKVNEMDSERLQYEKKLkstkslmaklssmkikvgqmqyekqrmeqkwETLKDELASLKEQLEEk 276
Cdd:pfam00038   95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKI-------------------------------ESLKEELAFLKKNHEE- 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769870  277 ecEVKRLQERLvcktkGEGVEILDRDENIKRKLKE--KNIEVQKMKKAVESLMAANEEKERKIEDLRQ 342
Cdd:pfam00038  143 --EVRELQAQV-----SDTQVNVEMDAARKLDLTSalAEIRAQYEEIAAKNREEAEEWYQSKLEELQQ 203
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
90-349 5.01e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 5.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870   90 MTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLnateEMLQQELLSRTSLETQK 169
Cdd:COG2433    385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI----ERLERELSEARSEERRE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  170 LELMAEISNLKlkltavekdrldyedrfrdtegliQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmq 249
Cdd:COG2433    461 IRKDREISRLD------------------------REIERLERELEEERERIEELKRKLERLKELWKLEHS--------- 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  250 yEKQRMEQKWETL-KDELASLKEQLEEKECEV----------KRLQERLVcKTKGEGVeILDR--DENIKRKLKEKNI-- 314
Cdd:COG2433    508 -GELVPVKVVEKFtKEAIRRLEEEYGLKEGDVvylrdasgagRSTAELLA-EAGPRAV-IVPGelSEAADEVLFEEGIpv 584

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  315 ------EVQKM-------KKAVESLMAANEE------KERKIEDLRQCLSRYRK 349
Cdd:COG2433    585 lpaedvTIQEVddlavvdEEELEAAIEDWEEraeerrREKKAEMLERLISEYRA 638
PTZ00121 PTZ00121
MAEBL; Provisional
 125-352 5.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  125 DQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGL- 203
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELk 1552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  204 -IQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVK 281
Cdd:PTZ00121  1553 kAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769870  282 RLQERLVCKTKGE---GVEILDRDENIKRKLKEKNIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQD 352
Cdd:PTZ00121  1633 KKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 732-779 5.25e-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: 5.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  732 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 779
Cdd:cd09504      3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 732-791 5.31e-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: 5.31e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769870  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09549      7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-242 5.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQG--EKIRDLEFCLEEHREKLnateEMLQQELLSRTSLETQKLELMAEISNLK 180
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQ 176

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769870  181 LKL-TAVEKDRLDYEDRFRDtegLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMK 242
Cdd:COG4717    177 EELeELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
Rabaptin pfam03528
Rabaptin;
103-312 6.79e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 40.09  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNLK-- 180
Cdd:pfam03528    7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVEL---DALQNQLALARAEMENIKav 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  181 ------LKLTAVEKDRLDYEDRFRDTEGLIQE-INDLRLKVN-EMDSERLQYEKKLKSTKSLMAKLSSM----------- 241
Cdd:pfam03528   84 atvsenTKQEAIDEVKSQWQEEVASLQAIMKEtVREYEVQFHrRLEQERAQWNQYRESAEREIADLRRRlsegqeeenle 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  242 -KIKVGQMQYEKQR-----MEQKWETLKDELASLKEQLEEKEC-EVKRLQERL----VCKTKGEG-VEILDRDENIKRKL 309
Cdd:pfam03528  164 dEMKKAQEDAEKLRsvvmpMEKEIAALKAKLTEAEDKIKELEAsKMKELNHYLeaekSCRTDLEMyVAVLNTQKSVLQED 243


                   ...
gi 1958769870  310 KEK 312
Cdd:pfam03528  244 AEK 246
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
 103-341 9.37e-03

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.


Pssm-ID: 462752 [Multi-domain]  Cd Length: 307  Bit Score: 39.18  E-value: 9.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE-FCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:pfam09311   15 QEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEdKMNQLSEETSNQVSTLAKRNQKSETLLDELQQAFSQAKRNFQD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  182 KLTAVEKDRLDYEDRF----RDTEGLIqeiNDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmQYEKQRMEQ 257
Cdd:pfam09311   95 QLAVLMDSREQVSDELvrlqKDNESLQ---GKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEV---RTAADHMEE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  258 KwetLKDELASLKEQLEEKECEVKRLQERLVcktkgegVEILDRDENIKrKLKEKNIEVQKMKKAVESLMAANEEKERKI 337
Cdd:pfam09311  169 K---LKAEILFLKEQIQAEQCLKENLEETLQ-------AEIENCKEEIA-SISSLKVELERIKAEKEQLENGLTEKIRQL 237


                   ....
gi 1958769870  338 EDLR 341
Cdd:pfam09311  238 EDLQ 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-230 9.39e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 9.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769870  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNAteemlqqellsrtsLETQKLELMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769870  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDlrlkvnEMDSERLQYEKKLKS 230
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEK------ELSKLQRELAEAEAQ 498
 
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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