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Conserved domains on  [gi|1958769872|ref|XP_038963640|]
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liprin-beta-1 isoform X4 [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 3.57e-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: 3.57e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  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 1.07e-37

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 1.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  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 3.10e-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: 122.34  E-value: 3.10e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769872  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 ...
 103-334 8.25e-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: 66.24  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLS 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 372-637 2.05e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  372 SDLERSTSSTP-GMGSPSRDPLHTSAPEEFHTSVLQASVPSlfptSMDEETCE---KPKLATKPETSFEEGDGRA-VLGA 446
Cdd:PHA03307   136 EMLRPVGSPGPpPAASPPAAGASPAAVASDAASSRQAALPL----SSPEETARapsSPPAEPPPSTPPAAASPRPpRRSS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  447 DAEVSLSDGVSTSSLQKSSSLGNlkkETSDGVEKESIQKP--PEDKTPTDSHTFGTLP-PKAPGHGASVDDSPFGTRKAR 523
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGA---SSSDSSSSESSGCGwgPENECPLPRPAPITLPtRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  524 SSFgrgffkikSGKRTASAPNLDRKRSASAPTLAETEKETDEHLDLAGTSRPKGSQGTSPFQMSPPSPDSRKKSRGIMRL 603
Cdd:PHA03307   289 SSP--------RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958769872  604 FGKLRRSqsttfnpddmSEPEFKRGGTRATAGPR 637
Cdd:PHA03307   361 DPSSPRK----------RPRPSRAPSSPAASAGR 384
 
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 3.57e-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: 3.57e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  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 1.07e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 1.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  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 3.10e-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: 122.34  E-value: 3.10e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769872  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 2.42e-18

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 80.01  E-value: 2.42e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  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 2.82e-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: 68.45  E-value: 2.82e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  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 8.45e-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: 61.54  E-value: 8.45e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769872   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 1.36e-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: 1.36e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 4.33e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.33e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-334 8.25e-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: 66.24  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLS 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-329 1.11e-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: 65.90  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   54 DLRGLLEMMETDEKEgLRCQIPDSTAEMLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  211 RLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvgqMQYEKQRMEQKWETLK---DELASLKEQLEE-------KECEV 280
Cdd:pfam05483  334 EAQMEELNKAKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKNEDQLKiitMELQKKSSELEEmtkfknnKEVEL 407

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  281 KRLQERLvcktkGEGVEILDRDIEVQKMKKAV----ESLMAANEEKERKIEDL 329
Cdd:pfam05483  408 EELKKIL-----AEDEKLLDEKKQFEKIAEELkgkeQELIFLLQAREKEIHDL 455
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-344 1.17e-09

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: 61.32  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  195 DRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWETLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  267 ASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQDPAA 344
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-338 1.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNE---MDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  258 KWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYR 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 1958769872  338 K 338
Cdd:PRK03918   419 K 419
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-884 6.43e-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: 47.68  E-value: 6.43e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   815 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 372-637 2.05e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  372 SDLERSTSSTP-GMGSPSRDPLHTSAPEEFHTSVLQASVPSlfptSMDEETCE---KPKLATKPETSFEEGDGRA-VLGA 446
Cdd:PHA03307   136 EMLRPVGSPGPpPAASPPAAGASPAAVASDAASSRQAALPL----SSPEETARapsSPPAEPPPSTPPAAASPRPpRRSS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  447 DAEVSLSDGVSTSSLQKSSSLGNlkkETSDGVEKESIQKP--PEDKTPTDSHTFGTLP-PKAPGHGASVDDSPFGTRKAR 523
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGA---SSSDSSSSESSGCGwgPENECPLPRPAPITLPtRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  524 SSFgrgffkikSGKRTASAPNLDRKRSASAPTLAETEKETDEHLDLAGTSRPKGSQGTSPFQMSPPSPDSRKKSRGIMRL 603
Cdd:PHA03307   289 SSP--------RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958769872  604 FGKLRRSqsttfnpddmSEPEFKRGGTRATAGPR 637
Cdd:PHA03307   361 DPSSPRK----------RPRPSRAPSSPAASAGR 384
 
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 3.57e-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: 3.57e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  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 1.07e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.13  E-value: 1.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  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 3.10e-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: 122.34  E-value: 3.10e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958769872  655 FAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 822-883 3.65e-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: 3.65e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  822 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 883
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 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 1958769872  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 3.24e-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: 3.24e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769872  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 2.42e-18

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 80.01  E-value: 2.42e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  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 6.24e-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: 6.24e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  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 1.61e-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: 1.61e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769872  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 2.82e-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: 68.45  E-value: 2.82e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  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 6.96e-13

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 64.18  E-value: 6.96e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958769872  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 1958769872  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 8.45e-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: 61.54  E-value: 8.45e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769872   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 1.36e-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: 1.36e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 4.33e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.33e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-334 8.25e-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: 66.24  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRFRDTEglIQEINDLRLKVNEMDSE---RLQ-YEKKLKSTKSLMAKLSS-MKIKVGQMQYEKQR--- 254
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRieaRLReIEQKLNRLTLEKEYLEKeIQELQEQRIDLKEQiks 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  255 MEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLS 334
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAALRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-329 1.11e-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: 65.90  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   54 DLRGLLEMMETDEKEgLRCQIPDSTAEMLIEWLQNQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLELMAEISNLKLKLT-AVEKDRLDYEDRFRDTEGLIQEINDL 210
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTICQLTEEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  211 RLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvgqMQYEKQRMEQKWETLK---DELASLKEQLEE-------KECEV 280
Cdd:pfam05483  334 EAQMEELNKAKAAHSFVVTEFEATTCSLEEL------LRTEQQRLEKNEDQLKiitMELQKKSSELEEmtkfknnKEVEL 407

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  281 KRLQERLvcktkGEGVEILDRDIEVQKMKKAV----ESLMAANEEKERKIEDL 329
Cdd:pfam05483  408 EELKKIL-----AEDEKLLDEKKQFEKIAEELkgkeQELIFLLQAREKEIHDL 455
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 662-717 1.01e-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: 1.01e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769872  662 QVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 717
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-344 1.17e-09

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: 61.32  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  195 DRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWETLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  267 ASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQDPAA 344
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-335 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 1958769872  103 QERLARLENDKESLVLQVSV-------LTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  176 ISNLKLKLTAVEKDRLDYEDRFRDT------------------EGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAK 237
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATerrledleeqieelsediESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  238 LSS----MKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcktkGEGVEILDRDIEvQKMKKAVE 313
Cdd:TIGR02168  892 LRSeleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL-----SEEYSLTLEEAE-ALENKIED 965

                          250       260
                   ....*....|....*....|..
gi 1958769872  314 SLMAAneekERKIEDLRQCLSR 335
Cdd:TIGR02168  966 DEEEA----RRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-320 3.70e-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: 60.84  E-value: 3.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK---LNATEEMLQ---QELLSR--------TSL 165
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEELEaqlEELESKldelaeelAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  166 ETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSM 241
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  242 KIKVGQMQYEKQRME--QKWETLKDELASLKEQLEEKECEVKRLQERLVcKTKGEGVEILDRDIEVQKMKKAVESLMAAN 319
Cdd:TIGR02168  423 IEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENL 501


                   .
gi 1958769872  320 E 320
Cdd:TIGR02168  502 E 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-338 1.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNE---MDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  258 KWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYR 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 1958769872  338 K 338
Cdd:PRK03918   419 K 419
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 5.29e-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: 5.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769872  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 ...
 155-355 7.45e-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: 7.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  155 LQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKL---KST 231
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  232 KSLMAklssmkikvgqMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKA 311
Cdd:COG1579     89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958769872  312 VESLMAANEEKERKI-EDLrqcLSRY---RKVQDPAALAQGQEGECEG 355
Cdd:COG1579    158 LEELEAEREELAAKIpPEL---LALYeriRKRKNGLAVVPVEGGACGG 202
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 102-329 1.91e-07

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: 55.03  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKLNATEEMLQQellsRTSLETQKLELMAEISNLKL 181
Cdd:TIGR04523  382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKET----IIKNNSEIKDLTNQDSVKEL 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  182 KLTAVEKDRLDYEDRFRDTEGLIQEIN--------DLRLKVNEMDSerLQYEKKL--KSTKSLMAKLSSMKIKVGQMQYE 251
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkELKSKEKELKK--LNEEKKEleEKVKDLTKKISSLKEKIEKLESE 532

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  252 KQRMEQKWETLKDELASLKEQLEEKECEvkrlqerlvcktkgegVEILDRDIEVQKMKKAVESLMAANEEKERKIEDL 329
Cdd:TIGR04523  533 KKEKESKISDLEDELNKDDFELKKENLE----------------KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 656-717 2.24e-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: 2.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  656 AKWTKEQVCSWL-AEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 717
Cdd:cd09564      2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-351 5.13e-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: 5.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLV------------------------LQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQ 157
Cdd:COG1196    234 LRELEAELEELEAELEeleaeleeleaelaeleaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  158 ELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRL-KVNEMDSERLQYEKKLKSTKSLMA 236
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeAEAELAEAEEELEELAEELLEALR 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  237 KLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLM 316
Cdd:COG1196    394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958769872  317 AANEEKERKIEDLRQCLSRYRKVQDPAALAQGQEG 351
Cdd:COG1196    474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 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 5.55e-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: 5.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769872  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 6.43e-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: 47.68  E-value: 6.43e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   815 VQQWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 104-331 8.72e-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: 53.19  E-value: 8.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  104 ERLARLENDKESLVLQVSvltdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSletqklelmaEISNLKLKL 183
Cdd:pfam05483  394 EEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  184 TAVEKDRLDYedrFRDTEGLIQEINDLRLKVNEM--DSERLQYEKK--LKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:pfam05483  460 TAIKTSEEHY---LKEVEDLKTELEKEKLKNIELtaHCDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769872  260 ETLKDELASLKEQLEEKECEVKRLQERLVCK-------TKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQ 331
Cdd:pfam05483  537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKldkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-288 9.62e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 9.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   81 MLIEWLQNQMTNGHLPgNGDVYQERLARLENDKEslvlQVSVLTDQVEAQGEKIRDLEfCLEEHREKLNATEEMLQQELl 160
Cdd:COG4717     46 MLLERLEKEADELFKP-QGRKPELNLKELKELEE----ELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREEL- 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  161 srtsletQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLkstKSLMAKLSS 240
Cdd:COG4717    119 -------EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL---EELLEQLSL 188

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769872  241 MKIK-VGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLV 288
Cdd:COG4717    189 ATEEeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-338 1.20e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  171 ELMAEISNLKLKLTAVEkdrlDYEDRFRDTEG----LIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVG 246
Cdd:PRK03918   173 EIKRRIERLEKFIKRTE----NIEELIKEKEKeleeVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  247 QMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQE-----RLVCKTKGEGVEILDRDIEVQKMK-------KAVES 314
Cdd:PRK03918   249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLsrleeeiNGIEE 328

                          170       180
                   ....*....|....*....|....
gi 1958769872  315 LMAANEEKERKIEDLRQCLSRYRK 338
Cdd:PRK03918   329 RIKELEEKEERLEELKKKLKELEK 352
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-333 1.21e-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: 52.87  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  132 EKIRDLEFCLEEHREKLNATEEMLQQEL----LSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  208 ndLRLKVNEMDSERLQYEKK-------LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWETL 262
Cdd:pfam01576  417 --LQARLSESERQRAELAEKlsklqseLESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQL 494

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  263 KDELASLKEQLEEKEcEVKRLQERLVCKTKgegVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCL 333
Cdd:pfam01576  495 EDERNSLQEQLEEEE-EAKRNVERQLSTLQ---AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 735-787 1.29e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.54  E-value: 1.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 787
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 120-331 1.45e-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: 52.38  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSR-TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFr 198
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRL- 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  199 dtEGLIQEINDLRLKVNEMDSER-LQYEKKLKSTKSlmaklssmkikvgqmqyekqrmeqkwetlkdELASLKEQLEEKE 277
Cdd:TIGR02169  268 --EEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEA-------------------------------EIASLERSIAEKE 314

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  278 CEVKRLQERLVC------KTKGEgVEILDRDIEVQKMKKavESLMAANEEKERKIEDLRQ 331
Cdd:TIGR02169  315 RELEDAEERLAKleaeidKLLAE-IEELEREIEEERKRR--DKLTEEYAELKEELEDLRA 371
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
731-791 1.55e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.49  E-value: 1.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  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 1.91e-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: 1.91e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09505      5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-354 2.01e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRfrdTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRMEQKWETL 262
Cdd:COG1196    388 LLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEAL 461

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  263 KDELASLKEQLEEKEcevKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIE----DLRQCLSRYRK 338
Cdd:COG1196    462 LELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavaVLIGVEAAYEA 538

                          250
                   ....*....|....*.
gi 1958769872  339 VQDPAALAQGQEGECE 354
Cdd:COG1196    539 ALEAALAAALQNIVVE 554
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-344 2.66e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  165 LETQKLELMAEISNLKLKLTAVEKDRLDYEDRfRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIK 244
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  245 VGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGV-----------EILDRDIEVQKMKKAVE 313
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralleerfaAALGDAVERELRENLEE 773

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958769872  314 SLMAANEEKERKIEDLRQCLSRYRKVQDPAA 344
Cdd:COG4913    774 RIDALRARLNRAEEELERAMRAFNREWPAET 804
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 7.24e-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: 7.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  655 FAKWTKEQVCSWLaEQGLGS---YLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09562      1 FALWNGPTVVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 654-719 8.37e-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: 8.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769872  654 PFAKWTKEQVCSWLAEQGLGSYLSS-GKHWImSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09507      1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-331 1.23e-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: 49.25  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEisnLKLKLTAVEK 188
Cdd:TIGR04523  300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  189 DRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWETLKDELAS 268
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----------EIERLKETIIKNNSEIKD 444

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  269 LKEQLEEKECEVKRL-QERLVCKTKGEGVEILDRDIE------VQKMKKAVESLMAANEEK---ERKIEDLRQ 331
Cdd:TIGR04523  445 LTNQDSVKELIIKNLdNTRESLETQLKVLSRSINKIKqnleqkQKELKSKEKELKKLNEEKkelEEKVKDLTK 517
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 64-356 1.97e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   64 TDEKEGLRCQIPDSTAEMliEWLQNQMTNghlpgNGDVYQERLARLEndkeSLVLQV-SVLTDQVEAQGEKIRDLEFCLE 142
Cdd:pfam15921  284 TEKASSARSQANSIQSQL--EIIQEQARN-----QNSMYMRQLSDLE----STVSQLrSELREAKRMYEDKIEELEKQLV 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  143 EHREKLnaTEEMLQQELLSRTS--LETQKLELMAEISNLKLKLTaVEKDRldyEDRF--RDTEGLIQeINDLRLKVNEMD 218
Cdd:pfam15921  353 LANSEL--TEARTERDQFSQESgnLDDQLQKLLADLHKREKELS-LEKEQ---NKRLwdRDTGNSIT-IDHLRRELDDRN 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  219 SERLQYEKKLKSTKSLMAklssmkikvGQMQYEKQRMEQKWETLkDELASLKEQLEEKECEVKRLQERLVCKTkgegvei 298
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQ---------GQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKK------- 488

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769872  299 ldrdIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYR-----KVQDPAALA------QGQEGECEGL 356
Cdd:pfam15921  489 ----MTLESSERTVSDLTASLQEKERAIEATNAEITKLRsrvdlKLQELQHLKnegdhlRNVQTECEAL 553
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-335 2.16e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSL-ETQKLEL 172
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  173 MAEISNLKLKLTAVEKDRLDYEDRFRDtegliqeindlrlkvneMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEK 252
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELED-----------------AEERLAKLEAEIDKLLAEIEELER---EIEEERKRR 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  253 QRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcKTKGEGVEILDRDIEvqKMKKAVESLMAANEEKERKIEDLRQC 332
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL--KDYREKLEKLKREIN--ELKRELDRLQEELQRLSEELADLNAA 428


                   ...
gi 1958769872  333 LSR 335
Cdd:TIGR02169  429 IAG 431
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-287 2.49e-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: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEML---------QQELLS-------RTSLE 166
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaeieeRREELGeraralyRSGGS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  167 TQKLELMAEISNLKlklTAVekDRLDYEDRFRDTEG-LIQEINDLRLKVNEmdsERLQYEKKLKSTKSLMAKLSSMKikv 245
Cdd:COG3883    102 VSYLDVLLGSESFS---DFL--DRLSALSKIADADAdLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAK--- 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958769872  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 ...
 163-334 4.00e-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: 47.71  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  163 TSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSlmaklssmk 242
Cdd:TIGR04523  169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ--------- 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  243 iKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLvcKTKGEGVEILDRDIEVQKMKKAVESLMAANEE- 321
Cdd:TIGR04523  240 -EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI--KELEKQLNQLKSEISDLNNQKEQDWNKELKSEl 316

                          170
                   ....*....|....*
gi 1958769872  322 --KERKIEDLRQCLS 334
Cdd:TIGR04523  317 knQEKKLEEIQNQIS 331
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
104-337 4.21e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKlnateemlqqellsRTSLETqkleLMAEISNLKLKL 183
Cdd:PRK02224   206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER--------------REELET----LEAEIEDLRETI 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  184 TAVEKDRLDYEDRFRD----TEGLIQEINDLRlkvNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:PRK02224   268 AETEREREELAEEVRDlrerLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  260 ETLKDELASLKEQLEEKECEVKRLQERL-----VCKTKGEGVEILDRDIEvqKMKKAVESLMAANEEKERKIEDLRQCLS 334
Cdd:PRK02224   345 ESLREDADDLEERAEELREEAAELESELeeareAVEDRREEIEELEEEIE--ELRERFGDAPVDLGNAEDFLEELREERD 422


                   ...
gi 1958769872  335 RYR 337
Cdd:PRK02224   423 ELR 425
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 1958769872  732 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09530      1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-376 4.54e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  109 LENDKESLVLQVSVLTdQVEAQGE-KIRDLEFCLEEHREKLNATEEmLQQELLSRTSLETQKLE-LMAEISNLKLKLTAV 186
Cdd:pfam01576  382 LESENAELQAELRTLQ-QAKQDSEhKRKKLEGQLQELQARLSESER-QRAELAEKLSKLQSELEsVSSLLNEAEGKNIKL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  187 EKDRLDYEDRFRDTEGLIQEINDLRL----KVNEMDSERLQYEKKL-----------KSTKSLMAKLSSMKIKVGQMQYE 251
Cdd:pfam01576  460 SKDVSSLESQLQDTQELLQEETRQKLnlstRLRQLEDERNSLQEQLeeeeeakrnveRQLSTLQAQLSDMKKKLEEDAGT 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  252 KQRMEQKWETLKDELASLKEQLEEKECEVKRLQerlvcKTKGE-GVEILDRDIEVQKMKKAVESLmaanEEKERKIEDL- 329
Cdd:pfam01576  540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-----KTKNRlQQELDDLLVDLDHQRQLVSNL----EKKQKKFDQMl 610

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958769872  330 ---RQCLSRYRKVQDPAAlAQGQEGECEGLFHSSSISTLLDAQgfSDLER 376
Cdd:pfam01576  611 aeeKAISARYAEERDRAE-AEAREKETRALSLARALEEALEAK--EELER 657
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 658-719 4.73e-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: 4.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09501      4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-287 4.76e-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: 47.07  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEE---MLQQELLS--------RTSLETQKLE 171
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAElekeiaelRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  172 L---------MAEISNLKLKLTAVEKD----RLDYEDRFrdTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:COG4942    106 LaellralyrLGRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769872  239 SSMKIKVGQMQYEKQRMEQKwetLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG4942    184 EEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-321 5.64e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 5.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEdrfRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLssmkikVGQMQYEKQRMEQKWEtl 262
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE------AEALENKIEDDEEEAR-- 971

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769872  263 kDELASLKEQLEE-------KECEVKRLQERLvcktkgegvEILDRDIEvqKMKKAVESLMAANEE 321
Cdd:TIGR02168  972 -RRLKRLENKIKElgpvnlaAIEEYEELKERY---------DFLTAQKE--DLTEAKETLEEAIEE 1025
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
198-354 5.91e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  198 RDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRME---------QKWETLKDELAS 268
Cdd:COG4717     64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAE 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  269 LKEQLEEKECEVKRLQERLvcktkgegVEILDRDIEVQKMKKAVESLMaaNEEKERKIEDLRQCLSRYRKVQDPAALAQG 348
Cdd:COG4717    144 LPERLEELEERLEELRELE--------EELEELEAELAELQEELEELL--EQLSLATEEELQDLAEELEELQQRLAELEE 213


                   ....*.
gi 1958769872  349 QEGECE 354
Cdd:COG4717    214 ELEEAQ 219
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
97-356 6.34e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 6.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   97 GNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEI 176
Cdd:PRK02224   342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  177 SNLKLKLTAVEKDRLDYEDRFRDTEGLIQE------------------INDLRLKVNEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:PRK02224   422 DELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  239 SSMKikvgqmqyekqRMEQKWETLKDELASLKEQLEEKECEVKRLQERlvCKTKGEGVEILDRDIEvQKMKKAVESLMAA 318
Cdd:PRK02224   502 EDLV-----------EAEDRIERLEERREDLEELIAERRETIEEKRER--AEELRERAAELEAEAE-EKREAAAEAEEEA 567

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958769872  319 NEEKE------RKIEDLRQCLSRYRKVQDPAALAQGQEGECEGL 356
Cdd:PRK02224   568 EEAREevaelnSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-350 7.58e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNL 179
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  180 KLKLTAVEKDRLDYEDRFRDTEGL-----------------IQEINDLRLKVNEMDSErlqyEKKLKSTKSLMAKLSSMK 242
Cdd:COG1340     98 RKELAELNKAGGSIDKLRKEIERLewrqqtevlspeeekelVEKIKELEKELEKAKKA----LEKNEKLKELRAELKELR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  243 IKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQErlvcktkgegveildrdiEVQKMKKAVESLMAANEEK 322
Cdd:COG1340    174 KEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK------------------EIVEAQEKADELHEEIIEL 235

                          250       260
                   ....*....|....*....|....*...
gi 1958769872  323 ERKIEDLRQCLSRYRKVQDPAALAQGQE 350
Cdd:COG1340    236 QKELRELRKELKKLRKKQRALKREKEKE 263
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 107-319 1.05e-04

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: 46.26  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  107 ARLENDKESLVLQVSVLTDQ---VEAQGEKIRDLEFCLEEHREKLNATEEMLQQeLLSRTSLETQKLE-LMAEISNLK-- 180
Cdd:pfam15921  468 AQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKERAIEATNAEITK-LRSRVDLKLQELQhLKNEGDHLRnv 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  181 ------LKLTAVEKD------RLDYEDRFR------DTEGLIQ--------EINDLRLKVNEMDSERLQYEKKLKSTKSL 234
Cdd:pfam15921  547 qteceaLKLQMAEKDkvieilRQQIENMTQlvgqhgRTAGAMQvekaqlekEINDRRLELQEFKILKDKKDAKIRELEAR 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  235 MAKLSSMKIK-----------VGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDI 303
Cdd:pfam15921  627 VSDLELEKVKlvnagserlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706

                          250
                   ....*....|....*.
gi 1958769872  304 EVQKMKKAVESLMAAN 319
Cdd:pfam15921  707 ELEQTRNTLKSMEGSD 722
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 141-339 1.14e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  141 LEEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDlRLKVNEMDSE 220
Cdd:TIGR04523  223 LKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  221 RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKgegveild 300
Cdd:TIGR04523  299 DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN-------- 370

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958769872  301 rdiEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKV 339
Cdd:TIGR04523  371 ---EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 106-275 1.20e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  106 LARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQ--ELLSRTSLETQKLELMAEISNLKLKL 183
Cdd:TIGR04523  498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQ 577

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  184 TAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmqyekqrmEQKWETLK 263
Cdd:TIGR04523  578 KSLKKKQEEKQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI----------KSKKNKLK 644

                          170
                   ....*....|..
gi 1958769872  264 DELASLKEQLEE 275
Cdd:TIGR04523  645 QEVKQIKETIKE 656
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
53-339 1.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   53 EDLRGLLEMMETDEKEglrcqiPDSTAEmLIEWLQNQmtNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQV----- 127
Cdd:PRK03918   217 PELREELEKLEKEVKE------LEELKE-EIEELEKE--LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkelke 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  128 -EAQGEKIRDLEFCLEEHREKLNATEEmlqqeLLSRTSLETQKLE-LMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQ 205
Cdd:PRK03918   288 lKEKAEEYIKLSEFYEEYLDELREIEK-----RLSRLEEEINGIEeRIKELEEKEERLEELKKKLKELEKRLEELEERHE 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  206 EINDLRLKVNEMdsERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKEcevKRLQE 285
Cdd:PRK03918   363 LYEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGK 437

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  286 RLVCK---TKGEGVEILDR-DIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKV 339
Cdd:PRK03918   438 CPVCGrelTEEHRKELLEEyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
658-719 1.34e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.10  E-value: 1.34e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  658 WTKEQVCSWLAEQGLGSYLSS-GKHWIMSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 42-328 1.43e-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: 46.12  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   42 FMGSLRALHLVEDLRGLLEMMETDEKEglrcqipdSTAEMLIEWLQNQMTNGHLPGNGDVYQERLARLENDKESLVLQ-- 119
Cdd:pfam02463  659 AEKSEVKASLSELTKELLEIQELQEKA--------ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQea 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  120 VSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKL--ELMAEISNLKLKLTAVEKDRLDYEDRF 197
Cdd:pfam02463  731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREktEKLKVEEEKEEKLKAQEEELRALEEEL 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  198 RDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWET--LKDELASLKEQLEE 275
Cdd:pfam02463  811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLkeEELEEQKLKDELES 890

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958769872  276 KECEVKR-LQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIED 328
Cdd:pfam02463  891 KEEKEKEeKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 1.78e-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: 1.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ 156
Cdd:pfam01519   26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 103-370 2.04e-04

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: 45.34  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  168 QklelMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMaklssmkikvgQ 247
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH-----------T 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  248 MQYEKQRMEQKWETLKDELASLKEQ--------LEEKECEVKRLQERLVCKTKGEGVEILDRDIE----VQKMKKAVESL 315
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQREqatidtrtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITctaqCEKLEKIHLQE 463

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  316 MA-ANEEKERKIEDLRQCLSRY-RKVQDPAALAQGQEGE----CEGLFHSSSISTLLDAQG 370
Cdd:TIGR00618  464 SAqSLKEREQQLQTKEQIHLQEtRKKAVVLARLLELQEEpcplCGSCIHPNPARQDIDNPG 524
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 372-637 2.05e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  372 SDLERSTSSTP-GMGSPSRDPLHTSAPEEFHTSVLQASVPSlfptSMDEETCE---KPKLATKPETSFEEGDGRA-VLGA 446
Cdd:PHA03307   136 EMLRPVGSPGPpPAASPPAAGASPAAVASDAASSRQAALPL----SSPEETARapsSPPAEPPPSTPPAAASPRPpRRSS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  447 DAEVSLSDGVSTSSLQKSSSLGNlkkETSDGVEKESIQKP--PEDKTPTDSHTFGTLP-PKAPGHGASVDDSPFGTRKAR 523
Cdd:PHA03307   212 PISASASSPAPAPGRSAADDAGA---SSSDSSSSESSGCGwgPENECPLPRPAPITLPtRIWEASGWNGPSSRPGPASSS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  524 SSFgrgffkikSGKRTASAPNLDRKRSASAPTLAETEKETDEHLDLAGTSRPKGSQGTSPFQMSPPSPDSRKKSRGIMRL 603
Cdd:PHA03307   289 SSP--------RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA 360

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958769872  604 FGKLRRSqsttfnpddmSEPEFKRGGTRATAGPR 637
Cdd:PHA03307   361 DPSSPRK----------RPRPSRAPSSPAASAGR 384
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-288 2.87e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  133 KIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDR------FRDTEGLIQE 206
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  207 INDLRLKVNEMDSERLQyekklkstksLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQER 286
Cdd:COG1579     98 IESLKRRISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                   ..
gi 1958769872  287 LV 288
Cdd:COG1579    168 LA 169
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-331 3.11e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  100 DVYQERLaRLENDKESLVLQVSVL-TDQVEAQ--GEKIRD--LEFCLEEHREKLNATEEMLQQELlsrTSLETQKLELMA 174
Cdd:COG3206    121 ERLRKNL-TVEPVKGSNVIEISYTsPDPELAAavANALAEayLEQNLELRREEARKALEFLEEQL---PELRKELEEAEA 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  175 EISNLKLK--LTAVEKDRLDYEDRFRDTEgliQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIkVGQMQYEK 252
Cdd:COG3206    197 ALEEFRQKngLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQL 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  253 QRMEQKWETLKD-------ELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERK 325
Cdd:COG3206    273 AELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352


                   ....*.
gi 1958769872  326 IEDLRQ 331
Cdd:COG3206    353 LRRLER 358
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 1958769872  735 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 792
Cdd:cd09547      6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-334 3.90e-04

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: 44.12  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   84 EWLQNQMtNGHLPGNGDVYQERLA---RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:pfam07888   30 ELLQNRL-EECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  161 SRTSLETQKLELMAEisnlklkltavekdRLDYEDRFRDTEGLIQEINDlRLKVNEMDSERLQyekklKSTKSLMAKLSS 240
Cdd:pfam07888  109 SSEELSEEKDALLAQ--------------RAAHEARIRELEEDIKTLTQ-RVLERETELERMK-----ERAKKAGAQRKE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  241 MKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERlVCKTKGEGVEILDRDIEVQKMKKAVESLMAANE 320
Cdd:pfam07888  169 EEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT-ITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247

                          250
                   ....*....|....
gi 1958769872  321 EKERKIEDLRQCLS 334
Cdd:pfam07888  248 ASERKVEGLGEELS 261
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-228 4.39e-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: 42.99  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEM------------LQQEL----LSRTSLE 166
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  167 TQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEG-LIQEINDLRLKVNEMDSERLQYEKKL 228
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAELEELEAEREELAAKI 172
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 732-791 4.85e-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: 4.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  732 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09552      6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-286 6.14e-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: 43.90  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellsrtsLETQKLELMAEISNLKLK 182
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD-------LESRLGDLKKERDELEAQ 897

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDrfrDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMkikvGQMQYEKQRMEQKWETL 262
Cdd:TIGR02169  898 LRELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL----EDVQAELQRVEEEIRAL 970

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958769872  263 --------------KDELASLKEQLEEKECEVKRLQER 286
Cdd:TIGR02169  971 epvnmlaiqeyeevLKRLDELKEKRAKLEEERKAILER 1008
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-286 6.36e-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: 6.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKLNATEEMLQQELLSRTSLETQKLElmAEISNLKLK 182
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIRGNGGDRLEQLE--REIERLERE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRfrdtegliqeINDLRLKVnemDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWETL 262
Cdd:COG4913    354 LEERERRRARLEAL----------LAALGLPL---PASAEEFAALRAEAAALLEALEE----------ELEALEEALAEA 410

                          170       180
                   ....*....|....*....|....
gi 1958769872  263 KDELASLKEQLEEKECEVKRLQER 286
Cdd:COG4913    411 EAALRDLRRELRELEAEIASLERR 434
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-350 6.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEF-CLEEHREKLNATEEMLQQELlsrtSLETQKLELMAEISNLKLK 182
Cdd:PRK03918   549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYNEYL----ELKDAEKELEREEKELKKL 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLqYEKKLKSTKSLMAKLSsmkikvgqmqyEKQRMEQKWETL 262
Cdd:PRK03918   625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL-REEYLELSRELAGLRA-----------ELEELEKRREEI 692

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  263 KDELASLKEQLEEKEcEVKRlqerlvcktkgegveildrdiEVQKMKKAVEslmaaneekerKIEDLRQCLSRYRKVQDP 342
Cdd:PRK03918   693 KKTLEKLKEELEERE-KAKK---------------------ELEKLEKALE-----------RVEELREKVKKYKALLKE 739


                   ....*...
gi 1958769872  343 AALAQGQE 350
Cdd:PRK03918   740 RALSKVGE 747
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-331 7.34e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  142 EEHREKLNATEEMLQQELLSRTSLETQ--KLELMAEisnlklkltAVEKDRlDYEDRFRDTEG--LIQEINDLRLKVNEM 217
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDILNELERQlkSLERQAE---------KAERYK-ELKAELRELELalLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  218 DSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL--VCKTKGEG 295
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEEL 321

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  296 VEILDRD---------------IEVQKMKKAVESLMAANEEKERKIEDLRQ 331
Cdd:TIGR02168  322 EAQLEELeskldelaeelaeleEKLEELKEELESLEAELEELEAELEELES 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 218-338 8.79e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  218 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL-----V 288
Cdd:COG3883     15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarA 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769872  289 CKTKGEGVEIL-------------------------DRDI--EVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRK 338
Cdd:COG3883     95 LYRSGGSVSYLdvllgsesfsdfldrlsalskiadaDADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 205-340 8.83e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 43.30  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  205 QEINDLRLKVNEMDSERLQYEkklkstkslMAKLSSMKiKVGQMQYEKQRMEQKWETLKD-ELASLKEQLEEKECEVKRL 283
Cdd:pfam06160   10 KEIDELEERKNELMNLPVQEE---------LSKVKKLN-LTGETQEKFEEWRKKWDDIVTkSLPDIEELLFEAEELNDKY 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769872  284 QERLVCKTKGEGVEILDrDIE--VQKMKKAVESLMAANEEKERKIEDLRQclsRYRKVQ 340
Cdd:pfam06160   80 RFKKAKKALDEIEELLD-DIEedIKQILEELDELLESEEKNREEVEELKD---KYRELR 134
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 1.04e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 38.85  E-value: 1.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  658 WTKEQVCSWLAEQ-GLGSYLSSGKHWIMSGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 714
Cdd:cd09504      5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
 103-330 1.04e-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: 42.26  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE-FCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKL 181
Cdd:pfam09311   15 QEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEdKMNQLSEETSNQVSTLAKRNQKSETLLDELQQAFSQAKRNFQD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  182 KLTAVEKDRLDYEDRF----RDTEGLIqeiNDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmQYEKQRMEQ 257
Cdd:pfam09311   95 QLAVLMDSREQVSDELvrlqKDNESLQ---GKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEV---RTAADHMEE 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769872  258 KwetLKDELASLKEQLEEKECEVKRLQERL---VCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLR 330
Cdd:pfam09311  169 K---LKAEILFLKEQIQAEQCLKENLEETLqaeIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDLQ 241
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 654-710 1.22e-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: 38.40  E-value: 1.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769872  654 PFAKWTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQQDLeKELGI-----KHSLHRK 710
Cdd:cd09512      3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 732-790 1.29e-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: 1.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09488      2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 111-323 1.30e-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: 42.11  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  111 NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDR 190
Cdd:pfam15905   73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQK 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  191 ----LDYEdrfrdtegLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLM----AKLSSMKIKVgqMQYEKQRMEQKWETL 262
Cdd:pfam15905  153 kmssLSME--------LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLehskGKVAQLEEKL--VSTEKEKIEEKSETE 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  263 -------------------KDELASLKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKE 323
Cdd:pfam15905  223 klleyitelscvseqvekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKE 302
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 103-354 1.46e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.50  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ------QELLSRTSLETQKLELMAEI 176
Cdd:pfam10174  365 TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkervKSLQTDSSNTDTALTTLEEA 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  177 SNLKLKLTAVEKDRLDYEDRFR--DTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKL-SSMKIKVGQMQYEKQ 253
Cdd:pfam10174  445 LSEKERIIERLKEQREREDRERleELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLaSSGLKKDSKLKSLEI 524

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  254 RMEQKwetlKDELASLKEQLeekecevKRLQERLVCKTKGEgvEILDR----DIEVQ-------KMKKAVESLMAANEE- 321
Cdd:pfam10174  525 AVEQK----KEECSKLENQL-------KKAHNAEEAVRTNP--EINDRirllEQEVArykeesgKAQAEVERLLGILREv 591

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958769872  322 ------KERKIEDLRQCLSRYRKVQdPAALAQGQEGECE 354
Cdd:pfam10174  592 enekndKDKKIAELESLTLRQMKEQ-NKKVANIKHGQQE 629
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
184-287 1.50e-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: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  184 TAVEKDRLDYEDRFRDTEGLIQ----EINDLRLKVNEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 259
Cdd:COG2433    402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467

                           90       100
                   ....*....|....*....|....*...
gi 1958769872  260 ETLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG2433    468 SRLDREIERLERELEEERERIEELKRKL 495
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
125-328 1.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  125 DQVEAQGEKIRDLEFCLEEHREKLNAT-EEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGL 203
Cdd:COG4372      2 DRLGEKVGKARLSLFGLRPKTGILIAAlSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  204 IQEIN--------DLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEE 275
Cdd:COG4372     82 LEELNeqlqaaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  276 KECEVKRLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIED 328
Cdd:COG4372    162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-339 1.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLvlqvsvlTDQVEAQGEKIRDLEFCLEEHREkLNATEEMLQQ--ELLSRTS-LETQKLELMA-EIS 177
Cdd:PRK03918   457 YTAELKRIEKELKEI-------EEKERKLRKELRELEKVLKKESE-LIKLKELAEQlkELEEKLKkYNLEELEKKAeEYE 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  178 NLKLKLTAVEKDRLDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKL-----KSTKSLMAKLSSMK------IKVG 246
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyneyLELK 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  247 QMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVCKTKGEGVE--------ILDRDIEVQKMKKAVESLMAA 318
Cdd:PRK03918   609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelreeYLELSRELAGLRAELEELEKR 688

                          250       260
                   ....*....|....*....|.
gi 1958769872  319 NEEKERKIEDLRQCLSRYRKV 339
Cdd:PRK03918   689 REEIKKTLEKLKEELEEREKA 709
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 658-702 2.02e-03

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


Pssm-ID: 188925  Cd Length: 66  Bit Score: 37.72  E-value: 2.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958769872  658 WTKEQVCSWLAEQGLGSYLSSGKHWIMSGQTLLQASQ---QDLEKELG 702
Cdd:cd09526      4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 170-329 2.05e-03

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: 40.66  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  170 LELMAEISNLKLKLTAVEKDRLDYEDRFRDTEgliQEINDLR-------LKVNEMDSERLQYEKKLKSTKSLMAKLSSMK 242
Cdd:pfam13851   22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTeplqkaqEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  243 IKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKR--------LQERLvcKTKGEGVEIldRDIEVQKMKKAV-- 312
Cdd:pfam13851   99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAAnl 174

                          170       180
                   ....*....|....*....|....*.
gi 1958769872  313 --ESLMAAN-------EEKERKIEDL 329
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 ...
 814-866 2.11e-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: 2.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958769872  814 EVQQWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 866
Cdd:cd09504      1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 112-331 2.37e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.73  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  112 DKESLVL----QVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEML----QQELLSRTSLE-TQKLELM--------- 173
Cdd:pfam10174  493 EKESSLIdlkeHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevaryke 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  174 ------AEISNLKLKLTAVEKDRLDYEDRFRDTEGLI--------QEINDLRLKVNEMDSERLQ-YEKKLKSTKSLMAKL 238
Cdd:pfam10174  573 esgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNS 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  239 SSMKIKVGQMQYEKQRmeQKWETLKDELASLKEQLEEKECEV--------KRLQERLVCKTKGEGVEILDRDIEV----- 305
Cdd:pfam10174  653 QQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDGHLtnlraerrKQLEEILEMKQEALLAAISEKDANIallel 730

                          250       260
                   ....*....|....*....|....*...
gi 1958769872  306 --QKMKKAVESLMAANEEKERKIEDLRQ 331
Cdd:pfam10174  731 ssSKKKKTQEEVMALKREKDRLVHQLKQ 758
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 162-289 2.49e-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: 38.75  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  162 RTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRfrdTEGLIQEindlrLKVNEMDSERLqyEKKLKSTKSLMAKLSSM 241
Cdd:pfam20492    1 REEAEREKQELEERLKQYEEETKKAQEELEESEET---AEELEEE-----RRQAEEEAERL--EQKRQEAEEEKERLEES 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958769872  242 KIKvgqMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVC 289
Cdd:pfam20492   71 AEM---EAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEE 115
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
119-343 2.49e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQqellsrtSLETQKLELMAEISNLKLKLTAVEKDRldyedrfr 198
Cdd:COG1340      2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELK-------ELAEKRDELNAQVKELREEAQELREKR-------- 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  199 dtEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWET----------LKDELAS 268
Cdd:COG1340     67 --DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlspeeekeLVEKIKE 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  269 LKEQLEEKECEVKRLQERLVCKTKGEGVEILDRDI----------------EVQKMKKAVESLMAANEEKERKIEDLRQC 332
Cdd:COG1340    145 LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIhkkikelaeeaqelheEMIELYKEADELRKEADELHKEIVEAQEK 224

                          250
                   ....*....|.
gi 1958769872  333 LSRYRKVQDPA 343
Cdd:COG1340    225 ADELHEEIIEL 235
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-303 2.56e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  105 RLARLENDKESLVLQVSVLTDQveaqgekirdlefcLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLT 184
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDE--------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  185 AVEKDRlDYEDRFRDTEGLIQEINDLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSmkikvgQMQYEKQRMEQKWETLKD 264
Cdd:COG1579     84 NVRNNK-EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA------ELEEKKAELDEELAELEA 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958769872  265 ELASLKEQLEEKECEV----KRLQERLVCKTKGEGVEILDRDI 303
Cdd:COG1579    157 ELEELEAEREELAAKIppelLALYERIRKRKNGLAVVPVEGGA 199
SAM_BAR cd09513
SAM domain of BAR subfamily; SAM (sterile alpha motif) domain of BAR (Bifunctional Apoptosis ...
 656-717 2.57e-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: 2.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769872  656 AKWTKEQVCSWLAEqgLGSYLSSGKHWIMS----GQTLLQASQQDLEKE-LGIKHSLHRKKLQLALQ 717
Cdd:cd09513      2 SKWTPEEVVLWLEQ--LGPWASLYRERFLSenvnGRLLLTLTEEELSKPpFNIENSLHRRAILTELE 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-331 3.05e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  147 KLNATEEMLQ------QELLSR-TSLETQK------LELMAEISNLKLKLTAVEKDRLD-----YEDRFRDTEGLIQEIN 208
Cdd:COG1196    180 KLEATEENLErledilGELERQlEPLERQAekaeryRELKEELKELEAELLLLKLRELEaeleeLEAELEELEAELEELE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  209 -DLRLKVNEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERL 287
Cdd:COG1196    260 aELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958769872  288 vcktKGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQ 331
Cdd:COG1196    340 ----EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 656-719 3.21e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 37.23  E-value: 3.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769872  656 AKWTKEQVCSWLAEQGLGSY--LSSGKHWImSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09515      2 HEWTCEDVAKWLKKEGFSKYvdLLCNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 104-331 3.24e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  104 ERLARLENDKESLVLQVSVLTdqVEAQGEKIRDLEFC-----LEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISN 178
Cdd:pfam17380  237 ERRKESFNLAEDVTTMTPEYT--VRYNGQTMTENEFLnqllhIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  179 LKlKLTAVEKDRLDYEDR----FRDTEGLIQEindlrlkvNEMDSERLQYEKKLKSTKSLMAKLSSMKI----KVGQMQY 250
Cdd:pfam17380  315 RR-KLEEAEKARQAEMDRqaaiYAEQERMAME--------RERELERIRQEERKRELERIRQEEIAMEIsrmrELERLQM 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  251 EKQrmeQKWETLKDEL-ASLKEQLEEKECEVK-RLQERLVCKTKGEGVEILDRDIEVQKMKKAVESLMAANEEKER--KI 326
Cdd:pfam17380  386 ERQ---QKNERVRQELeAARKVKILEEERQRKiQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERqqQV 462


                   ....*
gi 1958769872  327 EDLRQ 331
Cdd:pfam17380  463 ERLRQ 467
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 108-347 3.48e-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: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  108 RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLELMAEISNLKLKLTAVE 187
Cdd:pfam01576  205 ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  188 KDRLDYEDRFRDtegLIQEINDLRLKV----------NEMDSERLQYEKKLK-----STKSLMAKLSSMKIKVGQ----- 247
Cdd:pfam01576  285 AARNKAEKQRRD---LGEELEALKTELedtldttaaqQELRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQaleel 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  248 -------------MQYEKQRMEQKWETLKDELASLKEQLEEKECEVKR----LQERLVCKTKGEGV--EILDRdieVQKM 308
Cdd:pfam01576  362 teqleqakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKlegqLQELQARLSESERQraELAEK---LSKL 438

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958769872  309 KKAVESLMAANEEKERK-IEDLRQCLSRYRKVQDPAALAQ 347
Cdd:pfam01576  439 QSELESVSSLLNEAEGKnIKLSKDVSSLESQLQDTQELLQ 478
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 735-791 3.55e-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: 37.30  E-value: 3.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09505     10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 103-344 3.78e-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: 41.26  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMlqQELLSRTSLETQKLELMAEISNLKLK 182
Cdd:pfam05557   51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA--REVISCLKNELSELRRQIQRAELELQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  183 LTAVEKDRLdyedrfrdtegliQEINDL-RLKVNEMDSERLQYEKKLKStkslmakLSSMKIKVGQMQYEKQRMEQKWET 261
Cdd:pfam05557  129 STNSELEEL-------------QERLDLlKAKASEAEQLRQNLEKQQSS-------LAEAEQRIKELEFEIQSQEQDSEI 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  262 LKDELASLkEQLEEKECEVKRLQERLVC-KTKGEGVEILdrdievqkmkkaveslmaaNEEKerkiEDLRQCLSRYRKVQ 340
Cdd:pfam05557  189 VKNSKSEL-ARIPELEKELERLREHNKHlNENIENKLLL-------------------KEEV----EDLKRKLEREEKYR 244


                   ....
gi 1958769872  341 DPAA 344
Cdd:pfam05557  245 EEAA 248
Rabaptin pfam03528
Rabaptin;
103-331 3.89e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 40.86  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELlsrTSLETQKLELMAEISNLK-- 180
Cdd:pfam03528    7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVEL---DALQNQLALARAEMENIKav 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  181 ------LKLTAVEKDRLDYEDRFRDTEGLIQE-INDLRLKVN-EMDSERLQYEKKLKSTKSLMAKLSSM----------- 241
Cdd:pfam03528   84 atvsenTKQEAIDEVKSQWQEEVASLQAIMKEtVREYEVQFHrRLEQERAQWNQYRESAEREIADLRRRlsegqeeenle 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  242 -KIKVGQMQYEKQR-----MEQKWETLKDELASLKEQLEEKEC-EVKRLQERL----VCKTKGEG-VEILDRDIEVqkMK 309
Cdd:pfam03528  164 dEMKKAQEDAEKLRsvvmpMEKEIAALKAKLTEAEDKIKELEAsKMKELNHYLeaekSCRTDLEMyVAVLNTQKSV--LQ 241

                          250       260
                   ....*....|....*....|..
gi 1958769872  310 KAVESLMAANEEKERKIEDLRQ 331
Cdd:pfam03528  242 EDAEKLRKELHEVCHLLEQERQ 263
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 146-349 4.05e-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: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  146 EKLNATEEMLQ--QELLSRTSLETQKLE-----LMAEISNLKLKLTA-------VEKDRLDYEDRFRDTEGLIQEInDLR 211
Cdd:pfam01576    5 EEMQAKEEELQkvKERQQKAESELKELEkkhqqLCEEKNALQEQLQAetelcaeAEEMRARLAARKQELEEILHEL-ESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  212 LKVNEMDSERLQYEKKLKST--KSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQERLVC 289
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  290 KTkGEGVEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRY-RKVQDPAALAQGQ 349
Cdd:pfam01576  164 FT-SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAkRKLEGESTDLQEQ 223
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 656-704 4.33e-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: 36.89  E-value: 4.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958769872  656 AKWTKEQVCSWLaeQGLGS----YLSSGKHWIMSGQTLLQASQQDLEkELGIK 704
Cdd:cd09511      2 AKWSPKQVTDWL--KGLDDclqqYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 43-359 4.55e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872   43 MGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAEmliewLQNQMTNGHLPGngdVYQERLARLENDkeslVLQVSV 122
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPG---PLTRRMQRGEQT----YAQLET 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  123 LTDQVEAQGEKIRdlefcleEHREKLNATEEMLQQELLSRTSLETqklELMAEISNLkLKLTAVEKDRLDYEDRFRDTEG 202
Cdd:TIGR00618  543 SEEDVYHQLTSER-------KQRASLKEQMQEIQQSFSILTQCDN---RSKEDIPNL-QNITVRLQDLTEKLSEAEDMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  203 LIQEINDLRLKVNEMDSERLQYEK-------KLKSTKSLMA--------KLSSMKIKVGQMQY--EKQRMEQKWETLKDE 265
Cdd:TIGR00618  612 CEQHALLRKLQPEQDLQDVRLHLQqcsqelaLKLTALHALQltltqervREHALSIRVLPKELlaSRQLALQKMQSEKEQ 691

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  266 LASLKEQL----------EEKECEVKRLQERLVCKTKGEGVEILDRDIEVQK-----MKKAVESLMAANEEKERKIEDLR 330
Cdd:TIGR00618  692 LTYWKEMLaqcqtllrelETHIEEYDREFNEIENASSSLGSDLAAREDALNQslkelMHQARTVLKARTEAHFNNNEEVT 771

                          330       340
                   ....*....|....*....|....*....
gi 1958769872  331 QCLSRYRKVQDPAALAQGQEGECEGLFHS 359
Cdd:TIGR00618  772 AALQTGAELSHLAAEIQFFNRLREEDTHL 800
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 4.95e-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: 36.93  E-value: 4.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  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 5.81e-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: 36.38  E-value: 5.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958769872  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09549      7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-347 7.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  116 LVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLE-----TQKLELMAEISNLKLKLTAVEKDR 190
Cdd:COG4717    281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIEELQELLREAEELE 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  191 LDyedrfRDTEGLIQEINDLRLKVNEMDSERL-----QYEKKlkstKSLMAKLSSMKIKVGQMQYEKQRMEQKW--ETLK 263
Cdd:COG4717    361 EE-----LQLEELEQEIAALLAEAGVEDEEELraaleQAEEY----QELKEELEELEEQLEELLGELEELLEALdeEELE 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  264 DELASLKEQLEEKECEVKRLQERLVcKTKGEgVEILDRDIEVQKMKKAVESLMAANEEKERKI-------EDLRQCLSRY 336
Cdd:COG4717    432 EELEELEEELEELEEELEELREELA-ELEAE-LEQLEEDGELAELLQELEELKAELRELAEEWaalklalELLEEAREEY 509

                          250
                   ....*....|.
gi 1958769872  337 RKVQDPAALAQ 347
Cdd:COG4717    510 REERLPPVLER 520
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 103-353 7.64e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 7.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVS-VLTDQVEAQGEKIRDLE------------FCLEEHREKLNATEEMLQ--QELLSRTS--L 165
Cdd:pfam12128  652 RLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEaqlkqldkkhqaWLEEQKEQKREARTEKQAywQVVEGALDaqL 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  166 ETQKLELMAEISNLKLKLTAVEKDR--------LDYE---DRFRDTEGLIQEINDLRlkVNEmdSERLQYEKKLKSTKSL 234
Cdd:pfam12128  732 ALLKAAIAARRSGAKAELKALETWYkrdlaslgVDPDviaKLKREIRTLERKIERIA--VRR--QEVLRYFDWYQETWLQ 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  235 maklssmkikvgqmqyEKQRMEQKWETLKDELASLKEQLEEKECEVKRlqerlvcktkgegveildRDIEVQKMKKAVES 314
Cdd:pfam12128  808 ----------------RRPRLATQLSNIERAISELQQQLARLIADTKL------------------RRAKLEMERKASEK 853

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958769872  315 LMAANEEKERKIEDLRQCLSRYrKVQDPAALAQGQEGEC 353
Cdd:pfam12128  854 QQVRLSENLRGLRCEMSKLATL-KEDANSEQAQGSIGER 891
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-230 8.13e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNAteemlqqellsrtsLETQKLELMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769872  182 KLTAVEKDRLDYEDRFRDTEGLIQEINDlrlkvnEMDSERLQYEKKLKS 230
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEK------ELSKLQRELAEAEAQ 498
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 212-352 8.33e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  212 LKVNEM----DSERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWETLKDELASLKEQLEEKecevkrLQERL 287
Cdd:PRK00409   516 EKLNELiaslEELERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKE------AQQAI 579

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769872  288 VcKTKGEGVEILDRDIEVQKMKKAveslmaanEEKERKIEDLRQCLSRYRKVQDPAALAQGQEGE 352
Cdd:PRK00409   580 K-EAKKEADEIIKELRQLQKGGYA--------SVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 125-352 8.52e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 8.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  125 DQVEAQGEKIRDLEFCLEEHREKLNAteemLQQELlsrTSLETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEGLI 204
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDA----LQAEL---EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  205 QEindlRLKVNEMDSERLQYEKKLKSTKSLmaklSSMkikVGQMQYEKQRMEQKWETLkDELASLKEQLEEKECEVKRLQ 284
Cdd:COG3883     89 GE----RARALYRSGGSVSYLDVLLGSESF----SDF---LDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769872  285 ERLVCKTKgegvEILDRDIEVQKMKKAVESLMAANEEKERKIEDLRQCLSRYRKVQDPAALAQGQEGE 352
Cdd:COG3883    157 AELEALKA----ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 103-331 9.07e-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: 40.16  E-value: 9.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  103 QERLARLENDKESLVLQVSVLTDQVEA--------QGEK------IRDLE---FCLEEHREKLNATEEMLQQELLSRTS- 164
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqklQLEKvtteakIKKLEediLLLEDQNSKLSKERKLLEERISEFTSn 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  165 ----------LETQKLELMAEISNLKLKLTAVEKDRLDYEDRFRDTEG----LIQEINDLRLKVNEM------------- 217
Cdd:pfam01576  168 laeeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdLQEQIAELQAQIAELraqlakkeeelqa 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769872  218 -----DSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWETLKDELASLKEQLEEKECEVKRLQErlvCKTK 292
Cdd:pfam01576  248 alarlEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE---LRSK 324

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958769872  293 gegveildRDIEVQKMKKAVEslmaanEEK---ERKIEDLRQ 331
Cdd:pfam01576  325 --------REQEVTELKKALE------EETrshEAQLQEMRQ 352
 
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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