NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157837985|ref|NP_963922|]
View 

kazrin isoform E [Homo sapiens]

Protein Classification

SAM domain-containing protein; ACK family non-receptor tyrosine-protein kinase( domain architecture ID 10175987)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation| ACK (activated Cdc42-associated kinase) family non-receptor tyrosine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates; such as TNK1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 608-679 1.33e-43

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: 151.44  E-value: 1.33e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 608 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVF 679
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 443-512 9.90e-38

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: 134.89  E-value: 9.90e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 443 MSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 512
Cdd:cd09564    1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 522-586 9.88e-35

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: 126.37  E-value: 9.88e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 522 ELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 586
Cdd:cd09567    1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-261 2.01e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        170       180
                 ....*....|....*....|....
gi 157837985 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLL 497
 
Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 608-679 1.33e-43

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: 151.44  E-value: 1.33e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 608 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVF 679
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 443-512 9.90e-38

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: 134.89  E-value: 9.90e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 443 MSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 512
Cdd:cd09564    1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 522-586 9.88e-35

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: 126.37  E-value: 9.88e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 522 ELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 586
Cdd:cd09567    1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-261 2.01e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        170       180
                 ....*....|....*....|....
gi 157837985 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLL 497
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 532-585 3.18e-10

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: 56.51  E-value: 3.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837985  532 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 585
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 531-585 5.75e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.07  E-value: 5.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157837985   531 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 585
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-252 3.81e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    78 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 150
Cdd:TIGR02169  693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   151 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 222
Cdd:TIGR02169  773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|
gi 157837985   223 RSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLES 882
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 443-510 5.90e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 5.90e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985   443 MSHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRD 510
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
609-671 7.50e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.88  E-value: 7.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837985  609 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 671
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-240 1.01e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 155 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 224
Cdd:PRK02224 298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                        170
                 ....*....|....*.
gi 157837985 225 QLDLKDNRMKELEAEL 240
Cdd:PRK02224 378 AVEDRREEIEELEEEI 393
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 444-509 1.40e-06

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: 46.11  E-value: 1.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985  444 SHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLqLGLGVCSSLHRRKLRLAIEDYR 509
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 78-262 3.04e-06

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: 50.98  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 155
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  156 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 232
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 157837985  233 MKELEAELAMAKQSLATLTKDVPKRHSLAM 262
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 609-668 2.53e-04

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: 39.97  E-value: 2.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   609 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 668
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 125-251 3.72e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 125 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 203
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157837985 204 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 251
Cdd:cd22656  179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
 
Name Accession Description Interval E-value
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 608-679 1.33e-43

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: 151.44  E-value: 1.33e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 608 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVF 679
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 443-512 9.90e-38

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: 134.89  E-value: 9.90e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 443 MSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 512
Cdd:cd09564    1 MSRWKADMVLAWLEVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEEYRDPE 70
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 522-586 9.88e-35

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: 126.37  E-value: 9.88e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 522 ELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 586
Cdd:cd09567    1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 608-675 9.05e-24

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: 95.22  E-value: 9.05e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985 608 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEM 675
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHF 68
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 616-677 1.25e-21

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: 88.75  E-value: 1.25e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 616 RVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSA 677
Cdd:cd09496    1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 450-507 3.40e-21

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: 87.28  E-value: 3.40e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985 450 TVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 507
Cdd:cd09494    1 RVCAWLEDFGLMPMYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 527-586 1.85e-20

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 85.28  E-value: 1.85e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 527 WVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLY 586
Cdd:cd09495    1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
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 ...
 608-677 6.87e-20

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 84.29  E-value: 6.87e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 608 DPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSA 677
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNN 70
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 522-585 5.98e-18

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: 78.51  E-value: 5.98e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837985 522 ELDHHWVAKaWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEkHLNVSKKFHQVSILLGIELL 585
Cdd:cd09566    1 KLDTHWVLR-WLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVL 62
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 ...
 444-507 6.37e-15

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: 69.90  E-value: 6.37e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 444 SHWKAGTVQAWLEVVMAMPM-YVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 507
Cdd:cd09562    2 ALWNGPTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 66
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 ...
 523-585 1.23e-13

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: 66.34  E-value: 1.23e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837985 523 LDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 585
Cdd:cd09565    1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-261 2.01e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        170       180
                 ....*....|....*....|....
gi 157837985 238 AELAMAKQSLATLTKDVPKRHSLA 261
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLL 497
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 532-585 3.18e-10

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: 56.51  E-value: 3.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837985  532 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIELL 585
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 77-250 9.57e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 9.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQL--------------AQKEQELARAKEALQAMK 142
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaqaeeyellaelARLEQDIARLEERRRELE 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 143 ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF---IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHA 219
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                        170       180       190
                 ....*....|....*....|....*....|.
gi 157837985 220 TALRSQLDLKDNRMKELEAELAMAKQSLATL 250
Cdd:COG1196  396 AELAAQLEELEEAEEALLERLERLEEELEEL 426
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 446-507 4.00e-09

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: 53.39  E-value: 4.00e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 446 WKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIED 507
Cdd:cd09563    4 WSTEQVCDWLAE-LGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-245 4.56e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  15 AVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAatnmENPQLGAQV-LLREEVSRLQEEVHLLR 93
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE----ELAELEEELeELEEELEELEEELEEAE 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  94 QMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQL 173
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985 174 RDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQ 245
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 531-585 5.75e-09

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 53.07  E-value: 5.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157837985   531 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELL 585
Cdd:smart00454  11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-252 3.81e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    78 LREEVSRLQEEVHLLRQ-------MKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKG 150
Cdd:TIGR02169  693 LQSELRRIENRLDELSQelsdasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   151 EKTDLVSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAVKALAK-------EKDLLEREKWELRRQAKEATDHATAL 222
Cdd:TIGR02169  773 DLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|
gi 157837985   223 RSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEELEAALRDLES 882
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-252 5.79e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 5.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985     2 MEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNmenpqlgaqvLLREE 81
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----------QLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    82 VSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQ 161
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   162 LYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATD-------HATALRSQLDLKDNRMK 234
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNerasleeALALLRSELEELSEELR 904

                          250
                   ....*....|....*...
gi 157837985   235 ELEAELAMAKQSLATLTK 252
Cdd:TIGR02168  905 ELESKRSELRRELEELRE 922
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 443-510 5.90e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 49.99  E-value: 5.90e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985   443 MSHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRD 510
Cdd:smart00454   1 VSQWSPESVADWLES-IGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLKE 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-254 8.23e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.08  E-value: 8.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEmLAKDLEESQGGKssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLvs 157
Cdd:COG4913   240 AHEALEDAREQIELLEPIRE-LAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  158 qmQQLYATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:COG4913   315 --EARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                         170
                  ....*....|....*..
gi 157837985  238 AELAMAKQSLATLTKDV 254
Cdd:COG4913   387 AEAAALLEALEEELEAL 403
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 119-253 1.57e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 53.00  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDfIRNYEQhrkesedaVKALAKEK 198
Cdd:COG1579   28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKE--------YEALQKEI 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 199 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 253
Cdd:COG1579   99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-254 1.84e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    78 LREEVSRLQEEVHLLRQMKEMLAKDLEE-----SQGGKSSEVLSA---------TELRVQLAQKEQELARAKEALQAMKA 143
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISAlrkdlARLEAEVEQLEEriaqlskelTELEAEIEELEERLEEAEEELAEAEA 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   144 DRKRLKGEKTDLVSQMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAT---- 216
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeie 862

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 157837985   217 ---DHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:TIGR02168  863 eleELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-254 1.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   119 ELRVQLAQKEQELARAKEALQAMK---ADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 195
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985   196 K-------EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:TIGR02168  768 ErleeaeeELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 78-256 2.48e-07

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: 53.61  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLE--ESQGGKSSEVLSATElrVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:COG4942   32 LQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALE--QELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 156 VSQMQQL----YATLESREEQLRDFIRNYEQHRKesedAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN 231
Cdd:COG4942  110 LRALYRLgrqpPLALLLSPEDFLDAVRRLQYLKY----LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                        170       180
                 ....*....|....*....|....*
gi 157837985 232 RMKELEAELAMAKQSLATLTKDVPK 256
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAE 210
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
77-243 4.48e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKE-QELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALRE-------ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  156 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 235
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444


                  ....*...
gi 157837985  236 LEAELAMA 243
Cdd:COG4913   445 LRDALAEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-253 4.88e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLR-----QMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEK 152
Cdd:COG1196  218 LKEELKELEAELLLLKlreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 153 TDLVSQM---QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLK 229
Cdd:COG1196  298 ARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180
                 ....*....|....*....|....
gi 157837985 230 DNRMKELEAELAMAKQSLATLTKD 253
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQ 401
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
118-254 6.29e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 6.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 118 TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKE 197
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKE 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157837985 198 KDLLEREKWELRRQAKEatdhataLRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4372  124 RQDLEQQRKQLEAQIAE-------LQSEIAEREEELKELEEQLESLQEELAALEQEL 173
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
609-671 7.50e-07

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.88  E-value: 7.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837985  609 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEptFNAEAMAtALGIPSGKHilRRHL 671
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLR--LTLEDLK-RLGITSVGH--RRKI 58
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-250 8.13e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 8.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS----EVLSATELRV-----QLAQKEQELARAKEA---LQAMKADR 145
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDVasaerEIAELEAELERLDASsddLAALEEQL 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  146 KRLKGEKTDLVSQMQQLYATLESREEQLRDFirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 225
Cdd:COG4913   695 EELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770

                         170       180
                  ....*....|....*....|....*
gi 157837985  226 LdlkDNRMKELEAELAMAKQSLATL 250
Cdd:COG4913   771 L---EERIDALRARLNRAEEELERA 792
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-240 1.01e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSS-EVLSAT--ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREElETLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDD 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 155 LVSQ----------MQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRS 224
Cdd:PRK02224 298 LLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377

                        170
                 ....*....|....*.
gi 157837985 225 QLDLKDNRMKELEAEL 240
Cdd:PRK02224 378 AVEDRREEIEELEEEI 393
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 444-509 1.40e-06

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: 46.11  E-value: 1.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985  444 SHWKAGTVQAWLEVvMAMPMYVKACTENVKSGKVLLSLSDEDLqLGLGVCSSLHRRKLRLAIEDYR 509
Cdd:pfam00536   1 DGWSVEDVGEWLES-IGLGQYIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRLK 64
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-197 2.16e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   5 NKQLAlRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLLR-EEVS 83
Cdd:COG4942   54 LKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSpEDFL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  84 RLQEEVHLLRQMKEMLAKDLEESQggkssevlsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLY 163
Cdd:COG4942  133 DAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                        170       180       190
                 ....*....|....*....|....*....|....
gi 157837985 164 ATLESREEQLRDFIRNYEQHRKESEDAVKALAKE 197
Cdd:COG4942  202 ARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-255 2.37e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLE--RQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   156 VSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAlrsqldLKDNRMKE 235
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK------LEEAELKE 437

                          170       180
                   ....*....|....*....|
gi 157837985   236 LEAELAMAKQSLATLTKDVP 255
Cdd:TIGR02168  438 LQAELEELEEELEELQEELE 457
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 78-262 3.04e-06

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: 50.98  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSAtelrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDL-- 155
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQ--KKIENLQE-----QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLee 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  156 -VSQMQQLYATL-ESREEQLRDFIRNYEQHRKESEDAvkalaKEK-DLLEREKWELRRQAKEATDHATALRSQLDLKDNR 232
Cdd:pfam10174 444 aLSEKERIIERLkEQREREDRERLEELESLKKENKDL-----KEKvSALQPELTEKESSLIDLKEHASSLASSGLKKDSK 518

                         170       180       190
                  ....*....|....*....|....*....|
gi 157837985  233 MKELEAELAMAKQSLATLTKDVPKRHSLAM 262
Cdd:pfam10174 519 LKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 530-583 4.01e-06

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: 44.54  E-value: 4.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157837985 530 KAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSILLGIE 583
Cdd:cd09487    3 AEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKE-LGITSPGHRKKILRAIQ 55
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
78-248 4.81e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKEL 236
Cdd:COG4372  137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

                        170
                 ....*....|..
gi 157837985 237 EAELAMAKQSLA 248
Cdd:COG4372  217 AEELLEAKDSLE 228
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
77-252 8.50e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  77 LLREEVSRLQEEVHLLRQMKEMLAKDLEESQ----GGK----------SSEVLSATELRVQLAQKEQELARAKEALQAMK 142
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEalleAGKcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 143 ADRKRLKgektDLVSqmqqlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATAL 222
Cdd:PRK02224 496 ERLERAE----DLVE--------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563

                        170       180       190
                 ....*....|....*....|....*....|
gi 157837985 223 RSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER 593
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-254 1.26e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKtdlvsQMQQLYATLESREEQLRDFIRNYEQHRKEsEDAVKALAKEK 198
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEER-LEELRELEEEL 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837985 199 DLLEREKWELRRQAKEATDHATA--------LRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4717  166 EELEAELAELQEELEELLEQLSLateeelqdLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-254 1.29e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  121 RVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmQQLYATLESREEQLRDfIRNYEQHRKESEDAVKALAKEKDL 200
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837985  201 LErekwELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG4913   687 LA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
80-251 1.65e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  80 EEVSRLQEEVHLLRQMKEMLAKDLEESQGGKS--SEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKgektDLVS 157
Cdd:COG4717   88 EEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR----ELEE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM--KE 235
Cdd:COG4717  164 ELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAA 240

                        170
                 ....*....|....*.
gi 157837985 236 LEAELAMAKQSLATLT 251
Cdd:COG4717  241 LEERLKEARLLLLIAA 256
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 78-343 2.27e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGgkssevlSATELRVQLAQKEQELARAKEALQAMKADRKRlKGEKTDLVS 157
Cdd:COG3883   35 AQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREELGERARALYR-SGGSVSYLD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QM--QQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKE 235
Cdd:COG3883  107 VLlgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 236 LEAELAMAKQSLATL--TKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCH 313
Cdd:COG3883  187 LSAEEAAAEAQLAELeaELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266

                        250       260       270
                 ....*....|....*....|....*....|
gi 157837985 314 SRQPSVISDASAAEGDRSSTPSDINSPRHR 343
Cdd:COG3883  267 AAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 83-257 2.81e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  83 SRLQEEVHLLRQMKEMLAkDLEESQGGKSSEVlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKG---------EKT 153
Cdd:COG1579   17 SELDRLEHRLKELPAELA-ELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 154 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELrrqakeatdhatalrsqldlkDNRM 233
Cdd:COG1579   93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---------------------DEEL 151

                        170       180
                 ....*....|....*....|....
gi 157837985 234 KELEAELAMAKQSLATLTKDVPKR 257
Cdd:COG1579  152 AELEAELEELEAEREELAAKIPPE 175
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 123-214 4.22e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 123 QLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQlyatLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 202
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90
                 ....*....|..
gi 157837985 203 REKWELRRQAKE 214
Cdd:COG4942   97 AELEAQKEELAE 108
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 531-591 4.54e-05

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 41.92  E-value: 4.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157837985 531 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFS 591
Cdd:cd09505   12 TWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKSDS 72
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 119-247 5.05e-05

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: 43.37  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLyatlesreeqlrdfirnyEQHRKESEDAVKALAKEK 198
Cdd:pfam20492  10 ELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL------------------EQKRQEAEEEKERLEESA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157837985  199 DLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSL 247
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
78-265 6.18e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggksSEVLSATElrvQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:COG4372   43 LQEELEQLREELEQAREELEQLEEELEQAR----SELEQLEE---ELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQL---YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATalrsqldlkDNRMK 234
Cdd:COG4372  116 ELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---------EQALD 186

                        170       180       190
                 ....*....|....*....|....*....|.
gi 157837985 235 ELEAELAMAKQSLATLTKDVPKRHSLAMPGE 265
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELA 217
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-249 7.04e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATElrvqlaQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHE------ERREELETLEAEIEDLRETIAETEREREELAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEdavkALAKEKDLLEREKWELRR--------------QAKEATDHATALR 223
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELEDRDEELRDrleecrvaaqahneEAESLREDADDLE 355

                        170       180
                 ....*....|....*....|....*.
gi 157837985 224 SQLDLKDNRMKELEAELAMAKQSLAT 249
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVED 381
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
74-221 7.27e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   74 AQVLLREEVSRLQEEVHLLRQMKEMLAKDLEE------SQGGKSSEVLSA--TELRVQLAQKEQELARAKEALQAMKADR 145
Cdd:COG4913   296 ELEELRAELARLEAELERLEARLDALREELDEleaqirGNGGDRLEQLEReiERLERELEERERRRARLEALLAALGLPL 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  146 KRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKW-------ELRRQAKEATDH 218
Cdd:COG4913   376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALGL 455


                  ...
gi 157837985  219 ATA 221
Cdd:COG4913   456 DEA 458
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-255 8.12e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 8.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    78 LREEVSRLQEEVHLLRQMKEMLAKDleesqggkssevlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKE--------------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   158 QMQQLYATLESREEQLrdfirnyeqhrKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:TIGR02169  421 ELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489

                          170
                   ....*....|....*...
gi 157837985   238 AELAMAKQSLATLTKDVP 255
Cdd:TIGR02169  490 RELAEAEAQARASEERVR 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
103-254 9.59e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 103 LEESQGGKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADRK--RLKGEKTDLVSQMQQL---YATLESREEQLRDF 176
Cdd:COG3206  162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELesqLAEARAELAEAEAR 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985 177 IRNYEQHRKESEDAVKALAKEKDLLErekweLRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:COG3206  242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-225 1.03e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   17 QSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLlREEVSRLQEEVHLLRqmk 96
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-EREIAELEAELERLD--- 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   97 emlakdleesqggKSSEVLsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF 176
Cdd:COG4913   682 -------------ASSDDL--AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 157837985  177 IRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQ 225
Cdd:COG4913   747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 80-250 1.49e-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: 45.35  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    80 EEVSRLQEEVHLLrqmkemLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQm 159
Cdd:pfam02463  278 EKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK- 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   160 qqlYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQA----KEATDHATALRSQLDLKDNRMKE 235
Cdd:pfam02463  351 ---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKseeeKEAQLLLELARQLEDLLKEEKKE 427

                          170
                   ....*....|....*
gi 157837985   236 LEAELAMAKQSLATL 250
Cdd:pfam02463  428 ELEILEEEEESIELK 442
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-250 1.53e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 117 ATELRVQLAQKEQELARAKeaLQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDA------ 190
Cdd:COG1196  215 YRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeye 292

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837985 191 ----VKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATL 250
Cdd:COG1196  293 llaeLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 525-585 1.96e-04

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: 40.09  E-value: 1.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837985 525 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 585
Cdd:cd09507    3 TNWTTEevgAWLESLQLGEYRDIFARNDIRGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
PTZ00121 PTZ00121
MAEBL; Provisional
 74-239 2.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   74 AQVLLREEVSRLQEEVHLLRQMKEMLAKDL--EESQGGKSSEVLSATELRVQLAQ----------------KEQELARAK 135
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQlkkkeaeekkkaeelkKAEEENKIK 1662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  136 EALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRdfiRNYEQHRKESEDAVKA---LAKEKDLLEREKWELRRQA 212
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA---KKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEA 1739

                         170       180
                  ....*....|....*....|....*..
gi 157837985  213 KEATDHATALRSQLDLKdNRMKELEAE 239
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEK-KKIAHLKKE 1765
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 93-253 2.49e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    93 RQMKEMLAKDlEESQGGKSSEVLSATELRvQLAQKEQELARAKEALQamkadrKRLKGEkTDLVSQMQQLYATLESREEQ 172
Cdd:pfam01576    2 RQEEEMQAKE-EELQKVKERQQKAESELK-ELEKKHQQLCEEKNALQ------EQLQAE-TELCAEAEEMRARLAARKQE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   173 LRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152


                   .
gi 157837985   253 D 253
Cdd:pfam01576  153 E 153
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 609-668 2.53e-04

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: 39.97  E-value: 2.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   609 PVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTfnaEAMATALGIPSGKHILR 668
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTS---EEDLKELGITKLGHRKK 57
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
78-242 2.70e-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: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSatELRVQLAQKEQELARAKEALQ----AMKADRKRLKGEKT 153
Cdd:COG3206  228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 154 DLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKekdlLEREKWELRRQAKeatdhatALRSQLDLKDNRM 233
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-------VARELYESLLQRL 374


                 ....*....
gi 157837985 234 KELEAELAM 242
Cdd:COG3206  375 EEARLAEAL 383
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 78-215 2.73e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 44.36  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHL---LRQMKEMLAKDLEESQGGKSSEVlsATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTD 154
Cdd:pfam07111 486 LREERNRLDAELQLsahLIQQEVGRAREQGEAERQQLSEV--AQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAAS 563

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985  155 L---VSQMQQLY--------ATLESR-EEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK---WELRRQAKEA 215
Cdd:pfam07111 564 LrqeLTQQQEIYgqalqekvAEVETRlREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKernQELRRLQDEA 639
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 525-585 3.02e-04

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 39.55  E-value: 3.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157837985 525 HHWVAK---AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 585
Cdd:cd09575    3 HLWGTEevaAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 451-507 3.51e-04

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: 39.14  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157837985 451 VQAWLEVVmAMPMYVKACTENVKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 507
Cdd:cd09487    2 VAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-249 4.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   3 EDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLgaQVLLREEV 82
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL--EELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  83 SRLQEEVHLLRQMKEMLAKDLEESQggkssEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQL 162
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEE-----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 163 YATLESREEQLRDFIRNYEQH---RKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAE 239
Cdd:COG1196  486 LAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565

                        250
                 ....*....|
gi 157837985 240 LAMAKQSLAT 249
Cdd:COG1196  566 LKAAKAGRAT 575
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 80-254 4.69e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   80 EEVSRLQEEVHllrqMKEMLAKDLE---ESQGGKSSEV-LSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDL 155
Cdd:TIGR04523 440 SEIKDLTNQDS----VKELIIKNLDntrESLETQLKVLsRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  156 VSQMqqlyATLESREEQLRDFIRNYEQHRKESEDAVKAL--AKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRM 233
Cdd:TIGR04523 516 TKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591

                         170       180
                  ....*....|....*....|....*...
gi 157837985  234 KELEAE-------LAMAKQSLATLTKDV 254
Cdd:TIGR04523 592 DQKEKEkkdlikeIEEKEKKISSLEKEL 619
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 119-277 5.03e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  119 ELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA-KE 197
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKsKE 495

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  198 KDLLE--REKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLtKDVPKRHSLampgETVLNGNQEWV 275
Cdd:TIGR04523 496 KELKKlnEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD-DFELKKENL----EKEIDEKNKEI 570


                  ..
gi 157837985  276 VQ 277
Cdd:TIGR04523 571 EE 572
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 531-588 5.56e-04

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: 38.45  E-value: 5.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985 531 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLeKHLNVSKKFHQVSILLGIellYQV 588
Cdd:cd09533    4 DWLSSLGLPQYEDQFIENGITGDVLVALDHEDL-KEMGITSVGHRLTILKAV---YEL 57
PTZ00121 PTZ00121
MAEBL; Provisional
 74-239 6.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   74 AQVLLREEVSRLQEEVHLLRQMKEmlAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKT 153
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK--AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  154 DLVSQMQQLYATLESREEQLrdfIRNYEQHRKESEDAVKALAKEKDLLEREKW---ELRRQAKEATDHATALRSQLD--L 228
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEALKKEAEeaK 1702

                         170
                  ....*....|.
gi 157837985  229 KDNRMKELEAE 239
Cdd:PTZ00121 1703 KAEELKKKEAE 1713
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 80-256 7.60e-04

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: 43.17  E-value: 7.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   80 EEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATEL-----RVQLAQKE--QELARAKEALQAMKADRKRLKGEK 152
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdKLLLENKEltQEASDMTLELKKHQEDIINCKKQE 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  153 TDLVSQMQqlyaTLESREEQLRDFIRNYEQHRKESEDAVK---------ALAKEKDLLEREKW----------------- 206
Cdd:pfam05483 530 ERMLKQIE----NLEEKEMNLRDELESVREEFIQKGDEVKckldkseenARSIEYEVLKKEKQmkilenkcnnlkkqien 605

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985  207 ------ELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPK 256
Cdd:pfam05483 606 knknieELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-252 8.46e-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: 42.70  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  101 KDLEESQGGKSSEVLsatELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQmqqlyatlesreeqlrdfIRNY 180
Cdd:TIGR04523 345 SQLKKELTNSESENS---EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK------------------IQNQ 403

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157837985  181 EQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTK 252
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 66-324 9.68e-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: 42.80  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    66 NMENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKD---LEESQGGKSSEVLSAT-ELRVQLAQKEQELARAKEALQAM 141
Cdd:pfam15921  639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDyevLKRNFRNKSEEMETTTnKLKMQLKSAQSELEQTRNTLKSM 718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   142 K-ADRKRLK---GEKTDLVSQMQQLYAtLESREEQLrdfirnyeqhrkesEDAVKALAKEKDLLEREKWELRRQAKEATD 217
Cdd:pfam15921  719 EgSDGHAMKvamGMQKQITAKRGQIDA-LQSKIQFL--------------EEAMTNANKEKHFLKEEKNKLSQELSTVAT 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   218 HATALRSQLDL---KDNRMKELEA--ELAMAKQSLA-TLTKDVPKRHslampgetvlngnQEWVVQADLPLTAAIRQSQQ 291
Cdd:pfam15921  784 EKNKMAGELEVlrsQERRLKEKVAnmEVALDKASLQfAECQDIIQRQ-------------EQESVRLKLQHTLDVKELQG 850

                          250       260       270
                   ....*....|....*....|....*....|....
gi 157837985   292 TLYHSHPP-HPADRQAVRVSPCHSRQPSVISDAS 324
Cdd:pfam15921  851 PGYTSNSSmKPRLLQPASFTRTHSNVPSSQSTAS 884
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-255 9.71e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 9.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    16 VQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAatnmenPQLGAQV-LLREEVSRLqeevhllrq 94
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELsKLEEEVSRI--------- 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    95 mkEMLAKDLEESqggkssevLSATELRVQLAQKE-QELARAKEALQAMKADRKRlkgEKTDLVSQMQQLYATLESREEQL 173
Cdd:TIGR02169  811 --EARLREIEQK--------LNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAAL 877

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   174 RDfirnyeqhrkesedavkaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKD 253
Cdd:TIGR02169  878 RD------------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939


                   ..
gi 157837985   254 VP 255
Cdd:TIGR02169  940 KG 941
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 77-252 1.00e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    77 LLREEVSRLQEEvhllrQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLV 156
Cdd:pfam01576  196 LKKEEKGRQELE-----KAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   157 SQMQQLYATLESR-------EEQLRDFIRNYEQHRKESEDAVKALAKEKDL---LEREKWELRRQAKEATDHATALRSQL 226
Cdd:pfam01576  271 AQISELQEDLESEraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELrskREQEVTELKKALEEETRSHEAQLQEM 350

                          170       180
                   ....*....|....*....|....*..
gi 157837985   227 DLKDNR-MKELEAELAMAKQSLATLTK 252
Cdd:pfam01576  351 RQKHTQaLEELTEQLEQAKRNKANLEK 377
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
79-240 1.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  79 REEVSRLQEEVHLLRQMKEMLAKDLEESqggkssEVLSATELRVQ-LAQK----EQELARAKEALQAMKADRKRLKGEKT 153
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDRIErLEERredlEELIAERRETIEEKRERAEELRERAA 547

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 154 DLVSQMQQLYA---TLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLL------EREKWELRRQAKEATDHATALRS 224
Cdd:PRK02224 548 ELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRE 627

                        170
                 ....*....|....*.
gi 157837985 225 QLDLKDNRMKELEAEL 240
Cdd:PRK02224 628 RLAEKRERKRELEAEF 643
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 67-239 1.01e-03

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: 42.80  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985    67 MENPQLGAQVLLREEVSrlQEEVHLLRQMKEMLAK--------DLEESQGGK-----SSEVLSATELRVQLAQKEQELAR 133
Cdd:pfam15921  353 LANSELTEARTERDQFS--QESGNLDDQLQKLLADlhkrekelSLEKEQNKRlwdrdTGNSITIDHLRRELDDRNMEVQR 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   134 AKEALQAMKADRK--------RLKGeKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAK-EKDLLERE 204
Cdd:pfam15921  431 LEALLKAMKSECQgqmerqmaAIQG-KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDlTASLQEKE 509

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 157837985   205 KwelrrqAKEATD-HATALRSQLDLKDNRMKELEAE 239
Cdd:pfam15921  510 R------AIEATNaEITKLRSRVDLKLQELQHLKNE 539
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 65-235 1.17e-03

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: 42.40  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   65 TNMENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKdleesqggKSSEVLSATELRvqlAQKEQELARAKEAL---QAM 141
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK--------KSSELEEMTKFK---NNKEVELEELKKILaedEKL 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  142 KADRKRLKGEKTDLVSQMQQLYATLESREEQLRDF------IRNYEQH-RKESEDAVKALAKEK----------DLLERE 204
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeiqltaIKTSEEHyLKEVEDLKTELEKEKlknieltahcDKLLLE 500

                         170       180       190
                  ....*....|....*....|....*....|..
gi 157837985  205 KWELrrqAKEATDHATALRS-QLDLKDNRMKE 235
Cdd:pfam05483 501 NKEL---TQEASDMTLELKKhQEDIINCKKQE 529
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
123-244 1.20e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.17  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 123 QLAQKEQELARAKEALQAmKADRKRLKGEKtdlvsqmqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLE 202
Cdd:COG2268  238 RIAEAEAELAKKKAEERR-EAETARAEAEA-----------AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE 305

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157837985 203 -----REKWELRRQAKEATDHATALRSQLDLKdnrmKELEAELAMAK 244
Cdd:COG2268  306 leadvRKPAEAEKQAAEAEAEAEAEAIRAKGL----AEAEGKRALAE 348
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 78-228 1.23e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEMLAKDLEEsqggkssEVLSATElrvqlAQK--EQEL---ARAKEALQAMKADRKRLKGEK 152
Cdd:pfam07926   6 LQSEIKRLKEEAADAEAQLQKLQEDLEK-------QAEIARE-----AQQnyERELvlhAEDIKALQALREELNELKAEI 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985  153 TDLVSQMQQLYATLESREEqlrdfirnyeqhrkesedavkALAKEKDLLEREKWELRRQAKEATDHATALRSQLDL 228
Cdd:pfam07926  74 AELKAEAESAKAELEESEE---------------------SWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 442-512 1.25e-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: 38.07  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157837985 442 PMSHWKAGTVQAWLEVVMaMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAE 512
Cdd:cd09505    1 SLQDWSEEDVCTWLRSIG-LEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEELKMKS 70
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 120-255 1.52e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 120 LRVQLAQKEQELARAKEALQAMKADRKRLKGEKtDLVSQmqqlyatleSREEQLRDFIrnyEQHRKESEDAvkalakekd 199
Cdd:COG0542  402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ-DEASF---------ERLAELRDEL---AELEEELEAL--------- 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985 200 lleREKWElrrQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVP 255
Cdd:COG0542  460 ---KARWE---AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-253 1.57e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 116 SATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALA 195
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157837985 196 KEKDLLEREKWELRRQAKE--------ATDHATALRSQLDLKD--NRMKELEAELAMAKQSLATLTKD 253
Cdd:COG4942  101 AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAE 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-186 1.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   4 DNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENpQLGAQVLLREEVS 83
Cdd:COG1196  643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE-LAEAEEERLEEEL 721

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  84 RLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQA-----MKADR--KRLKGEKTDLV 156
Cdd:COG1196  722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnLLAIEeyEELEERYDFLS 801

                        170       180       190
                 ....*....|....*....|....*....|
gi 157837985 157 SQmqqlYATLESREEQLRDFIRNYEQHRKE 186
Cdd:COG1196  802 EQ----REDLEEARETLEEAIEEIDRETRE 827
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 612-665 1.75e-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: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157837985 612 WTNQRVLKW-VRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKH 665
Cdd:cd09504    5 WTVEDTVEWlVNSVELPQYVEAFKENGVDGSALPRLAVNNPSFLTSVLGIKDPIH 59
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 78-215 1.81e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEAL---------QAMKADRKRL 148
Cdd:COG1579   22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyEALQKEIESL 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157837985 149 KGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEA 215
Cdd:COG1579  102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 86-202 1.97e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 39.88  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   86 QEEVHLLRQMKEMLAKDLEESQGgKSSEVLSATELRVQLAQKEQE-LARAKEALQAMKADRKRLKGEKtdLVSQMQQLYA 164
Cdd:pfam10368  32 KKEQELYEEIIELGMDEFDEIKK-LSDEALENVEEREELLEKEKEsIEEAKEEFKKIKEIIEEIEDEE--LKKEAEELID 108

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 157837985  165 TLESREEQLRDFIRNYEqhrkesedavKALAKEKDLLE 202
Cdd:pfam10368 109 AMEERYEAYDELYDAYK----------KALELDKELYE 136
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 119-251 2.29e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  119 ELRVQLAQKEQELARA---KEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHR----------K 185
Cdd:pfam00529  62 SAEAQLAKAQAQVARLqaeLDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiggisrE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  186 ESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDN----RMKELEAELAMAKQSLATLT 251
Cdd:pfam00529 142 SLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlQIAEAEAELKLAKLDLERTE 211
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-244 2.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEEsQGGKSSEVLSATELRVQLAQKEQ-ELARAKEALQAMKADRKRLKGEKTDLV 156
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEE-LGFESVEELEERLKELEPFYNEYlELKDAEKELEREEKELKKLEEELDKAF 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 157 SQMQQLYATLESREEQLRDFIRNY--EQHRKESEDAVKaLAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMK 234
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYseEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711

                        170
                 ....*....|.
gi 157837985 235 ELEA-ELAMAK 244
Cdd:PRK03918 712 ELEKlEKALER 722
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 117-291 2.90e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  117 ATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNY-------EQHRKESED 189
Cdd:pfam07888  29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheelEEKYKELSA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  190 AVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKD---NRMKE------------------LEAELAMAKQSLA 248
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelERMKErakkagaqrkeeeaerkqLQAKLQQTEEELR 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 157837985  249 TLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQ 291
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
78-244 3.61e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 158 QMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLErekwELRRQAKEATDHATALRSQLDLKDNRMKELE 237
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAE 446


                 ....*..
gi 157837985 238 AELAMAK 244
Cdd:PRK02224 447 ALLEAGK 453
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
80-205 3.69e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  80 EEVSRLQEEVHLLRQMKEMLAKDLEESQggKSSEVLSATELrvqlaqkEQELARAKEALQAMKADRKRLKGEKTDLVSQM 159
Cdd:COG4717  392 EQAEEYQELKEELEELEEQLEELLGELE--ELLEALDEEEL-------EEELEELEEELEELEEELEELREELAELEAEL 462

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157837985 160 QQL-----YATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREK 205
Cdd:COG4717  463 EQLeedgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 125-251 3.72e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 125 AQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLrdfirnyeqhrKESEDAVKA-LAKEKDLLER 203
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL-----------ETLEKALKDlLTDEGGAIAR 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157837985 204 EKWE-LRRQAKEAT-DHATALRSQLDLKDNRMKELEAELAMAKQSLATLT 251
Cdd:cd22656  179 KEIKdLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 532-570 3.75e-03

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.51  E-value: 3.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157837985 532 WLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVS 570
Cdd:cd09501   12 WLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMS 50
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 121-254 4.18e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 40.44  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  121 RVQLAQKEQELARAKEALQAMKADRKRLkgekTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDL 200
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGL----TRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157837985  201 LEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDV 254
Cdd:pfam19220 123 LERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQEN 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-255 4.56e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 129 QELARAKEALQAMKADRKRLKgEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRkesedAVKALAKEKDLLEREKWEL 208
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAEL 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157837985 209 RRQAKEATDHATALRSQLdlkdNRMKELEAELAMAKQSLATLTKDVP 255
Cdd:COG4717  145 PERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLS 187
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 525-563 4.71e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 36.46  E-value: 4.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157837985 525 HHW----VAKaWLNDIGLSQYSQAF-QNHLVDGRMLNSLMKRDL 563
Cdd:cd09515    2 HEWtcedVAK-WLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 103-198 5.22e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.66  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 103 LEESQGGKSSEvlsaTELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDlvSQMQQLYATLESREEQLRDFIRNYEQ 182
Cdd:COG2825   35 LQESPEGKAAQ----KKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSE--EERQKKERELQKKQQELQRKQQEAQQ 108

                         90       100
                 ....*....|....*....|....*...
gi 157837985 183 --HRKESE----------DAVKALAKEK 198
Cdd:COG2825  109 dlQKRQQEllqpilekiqKAIKEVAKEE 136
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
532-585 5.66e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 36.09  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157837985  532 WLNDIGLSQYSQAFQNHLVDG-RMLNSLMKRDLeKHLNVSKKFHQVSILLGIELL 585
Cdd:pfam07647  12 WLRSIGLEQYTDNFRDQGITGaELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
79-248 5.67e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  79 REEvsrLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQ 158
Cdd:PRK02224 274 REE---LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 159 MqqlyATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRR-------QAKEATDHATALRSQLDLKDN 231
Cdd:PRK02224 351 A----DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELRE 426

                        170
                 ....*....|....*..
gi 157837985 232 RMKELEAELAMAKQSLA 248
Cdd:PRK02224 427 REAELEATLRTARERVE 443
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 84-279 5.93e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  84 RLQEEVHLLRQMKEMLAKDLEesqggKSSEVLSATE-LRVQLAQKEQELARAKEALQAMKADrkrlkgektdlvsqMQQL 162
Cdd:PRK00409 496 RLGLPENIIEEAKKLIGEDKE-----KLNELIASLEeLERELEQKAEEAEALLKEAEKLKEE--------------LEEK 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 163 YATLESREEQLRdfirnyEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEAtdhatalrsqldLKDNRMKELEAELAM 242
Cdd:PRK00409 557 KEKLQEEEDKLL------EEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS------------VKAHELIEARKRLNK 618

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157837985 243 AKQSLATLTKDVPKRHSLAMPGETV-------------LNGNQEWVVQAD 279
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgevlsIPDDKEAIVQAG 668
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 442-507 7.27e-03

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: 35.85  E-value: 7.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157837985 442 PMSHWKAGTVQAWLEvVMAMPMYVKACTENVKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 507
Cdd:cd09507    1 PVTNWTTEEVGAWLE-SLQLGEYRDIFARNDIRGSELLHLERRDLK-DLGITKVGHVKRILQAIKD 64
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 78-240 7.62e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985  78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVL---------SATELRVQLAQKEQELARAKEALQAMKADRKRL 148
Cdd:COG5185  287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEqeleeskreTETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985 149 KGE--KTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKEsedAVKALAKEKDLLEREKWELRRQAKEATdhatalrSQL 226
Cdd:COG5185  367 VGEveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQAT-------SSN 436

                        170
                 ....*....|....
gi 157837985 227 DLKDNRMKELEAEL 240
Cdd:COG5185  437 EEVSKLLNELISEL 450
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 78-202 8.27e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 37.28  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157837985   78 LREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVS 157
Cdd:pfam10473   8 VLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTK 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157837985  158 QMQQLYAT---LESREEQLRDFIRNYEQHR----KESEDAVKALAKE-KDLLE 202
Cdd:pfam10473  88 ELQKKQERvseLESLNSSLENLLEEKEQEKvqmkEESKTAVEMLQTQlKELNE 140
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 531-578 8.43e-03

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: 35.37  E-value: 8.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157837985 531 AWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKhLNVSKKFHQVSI 578
Cdd:cd09506   12 DWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTE-LGVTRVGHRMNI 58
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
446-507 8.73e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 35.32  E-value: 8.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157837985  446 WKAGTVQAWLEVvMAMPMYVKACTEN-VKSGKVLLSLSDEDLQlGLGVCSSLHRRKLRLAIED 507
Cdd:pfam07647   4 WSLESVADWLRS-IGLEQYTDNFRDQgITGAELLLRLTLEDLK-RLGITSVGHRRKILKKIQE 64
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 525-555 9.20e-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: 35.77  E-value: 9.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157837985 525 HHWVAK---AWL-NDIGLSQYSQAFQNHLVDGRML 555
Cdd:cd09504    3 HNWTVEdtvEWLvNSVELPQYVEAFKENGVDGSAL 37
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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