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Conserved domains on  [gi|213972596|ref|NP_001094052|]
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liprin-beta-2 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 714-785 1.62e-44

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.62e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 629-691 1.09e-37

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.74  E-value: 1.09e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 629 LLDHVWVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09566    1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 555-618 5.81e-35

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: 126.96  E-value: 5.81e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972596 555 FAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-316 1.49e-11

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.54  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    59 LALEMLALPQEREALLSQIpgptaayikewfEDSLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   219 VEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSA----LHSDHAERDQEIHRLKmgMETLRVANED 294
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrrerLQQEIEELLKKLEEAE--LKELQAELEE 444

                          250       260
                   ....*....|....*....|..
gi 213972596   295 KDRRIEELTGLLNQYLRVKEIV 316
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEEL 466
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 714-785 1.62e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.62e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 629-691 1.09e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.74  E-value: 1.09e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 629 LLDHVWVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09566    1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 555-618 5.81e-35

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: 126.96  E-value: 5.81e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972596 555 FAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 634-690 3.67e-16

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 73.46  E-value: 3.67e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596  634 WVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 557-619 3.49e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 70.76  E-value: 3.49e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596  557 QWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 619
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 555-619 2.44e-13

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: 65.39  E-value: 2.44e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972596   555 FAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
715-785 6.64e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596  715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 785
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-316 1.49e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.54  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    59 LALEMLALPQEREALLSQIpgptaayikewfEDSLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   219 VEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSA----LHSDHAERDQEIHRLKmgMETLRVANED 294
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrrerLQQEIEELLKKLEEAE--LKELQAELEE 444

                          250       260
                   ....*....|....*....|..
gi 213972596   295 KDRRIEELTGLLNQYLRVKEIV 316
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEEL 466
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 108-354 6.18e-09

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: 60.13  E-value: 6.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLSRSSAL 267
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIENMTQL 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   268 HSDH-----------AERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQyLRVKEIVMATQGsSERTLSINE----- 331
Cdd:pfam15921  578 VGQHgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKDikqer 655

                          250       260
                   ....*....|....*....|....*..
gi 213972596   332 ----DEIEGSFRKWNTTSKSpEEVMKQ 354
Cdd:pfam15921  656 dqllNEVKTSRNELNSLSED-YEVLKR 681
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-341 2.62e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  68 QEREALLsqipgptAAYIKEWFEDSLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEV 144
Cdd:COG1196  223 KELEAEL-------LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 145 CLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELEN 224
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 225 ERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS----RSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIE 300
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEalleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 213972596 301 ELTGLLNQYLR-VKEIVMATQGSSERTLSINEDEIEGSFRKW 341
Cdd:COG1196  453 ELEEEEEALLElLAELLEEAALLEAALAELLEELAEAAARLL 494
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 715-784 4.89e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.37  E-value: 4.89e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 784
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 635-690 4.94e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.37  E-value: 4.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596   635 VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-354 7.16e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 7.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 163 ELLSRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVA 241
Cdd:PRK03918 452 ELLEEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYE 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 242 QLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLK------------MGMETLrvanEDKDRRIEELTGLLNQY 309
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEeelaellkeleeLGFESV----EELEERLKELEPFYNEY 604

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 213972596 310 LRVKEIVMATQgSSERTLSINEDEIEGSFRKWNTTSKSPEEVMKQ 354
Cdd:PRK03918 605 LELKDAEKELE-REEKELKKLEEELDKAFEELAETEKRLEELRKE 648
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 714-785 1.62e-44

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 154.54  E-value: 1.62e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09569    1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 629-691 1.09e-37

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 134.74  E-value: 1.09e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 629 LLDHVWVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09566    1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 555-618 5.81e-35

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: 126.96  E-value: 5.81e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972596 555 FAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
Cdd:cd09563    1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 722-783 1.15e-29

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 111.86  E-value: 1.15e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 722 RVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNA 783
Cdd:cd09496    1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 714-785 2.43e-29

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 111.38  E-value: 2.43e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09570    1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 634-691 3.72e-27

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: 104.54  E-value: 3.72e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596 634 WVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLL-FLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09495    2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLvHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 562-618 2.17e-25

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: 99.61  E-value: 2.17e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 213972596 562 RVCTWLQDFGLAQ-YVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKA 618
Cdd:cd09494    1 RVCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 714-785 7.07e-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: 7.07e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 714 EVVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEPRFTGDTLAMLLNIPPQKTLLRRHLTTKFNALI 785
Cdd:cd09568    1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 634-690 3.67e-16

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 73.46  E-value: 3.67e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596  634 WVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:pfam00536   7 DVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 557-619 3.49e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 70.76  E-value: 3.49e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596  557 QWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKeLGIKHPLHRKKLVLAVKAI 619
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 629-691 1.63e-14

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: 68.98  E-value: 1.63e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972596 629 LLDHVWVTR-WLDDIGLPQYKDQFYESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVLH 691
Cdd:cd09567    1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLeKHLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 555-619 2.44e-13

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: 65.39  E-value: 2.44e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972596   555 FAQWSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
715-785 6.64e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 61.52  E-value: 6.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596  715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILepRFTGDTLAmllNIPPQKTLLRRHLTTKFNALI 785
Cdd:pfam07647   1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLK---RLGITSVGHRRKILKKIQELK 66
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 562-617 1.05e-11

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: 60.33  E-value: 1.05e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972596 562 RVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 617
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-316 1.49e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.54  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    59 LALEMLALPQEREALLSQIpgptaayikewfEDSLSQVNHHSAASNEtYQERLARLEGDKESLILQVSVLTDQVEAQGEK 138
Cdd:TIGR02168  230 LVLRLEELREELEELQEEL------------KEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   139 IRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIK 218
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL----------EELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   219 VEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSA----LHSDHAERDQEIHRLKmgMETLRVANED 294
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrrerLQQEIEELLKKLEEAE--LKELQAELEE 444

                          250       260
                   ....*....|....*....|..
gi 213972596   295 KDRRIEELTGLLNQYLRVKEIV 316
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEEL 466
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 634-687 2.22e-11

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: 59.56  E-value: 2.22e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 213972596 634 WVTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAI 687
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-302 4.29e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 4.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   128 LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQellsrtsLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEE 207
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQ-------LRKELEELSRQISALRKDL---ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   208 LLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQValkDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGMET 287
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                          170
                   ....*....|....*
gi 213972596   288 LRVANEDKDRRIEEL 302
Cdd:TIGR02168  829 LERRIAATERRLEDL 843
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 630-690 6.54e-10

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 55.94  E-value: 6.54e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 630 LDHVWV-TRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDL-LFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09565    1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLrTHLKMVDSFHRTSLQYGILCL 63
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 108-354 6.18e-09

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: 60.13  E-value: 6.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   108 QERLARLEGDKESLiLQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKlk 187
Cdd:pfam15921  447 ERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR-- 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 lvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENernqyewelkaTKAEVAQLQEQVALKDAEIERLHSQLSRSSAL 267
Cdd:pfam15921  524 ---------------SRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKDKVIEILRQQIENMTQL 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   268 HSDH-----------AERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQyLRVKEIVMATQGsSERTLSINE----- 331
Cdd:pfam15921  578 VGQHgrtagamqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-LELEKVKLVNAG-SERLRAVKDikqer 655

                          250       260
                   ....*....|....*....|....*..
gi 213972596   332 ----DEIEGSFRKWNTTSKSpEEVMKQ 354
Cdd:pfam15921  656 dqllNEVKTSRNELNSLSED-YEVLKR 681
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-341 2.62e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  68 QEREALLsqipgptAAYIKEWFEDSLSQVN---HHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEV 144
Cdd:COG1196  223 KELEAEL-------LLLKLRELEAELEELEaelEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 145 CLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELEN 224
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 225 ERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS----RSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIE 300
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEalleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 213972596 301 ELTGLLNQYLR-VKEIVMATQGSSERTLSINEDEIEGSFRKW 341
Cdd:COG1196  453 ELEEEEEALLElLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-309 2.80e-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: 57.77  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    53 LIEDLRLALEmlalpqEREALLSQIpgptAAYIKEWFEDSLSQVnhhsaasnetyQERLARLEGDKESLILQVSVLTDQV 132
Cdd:TIGR02169  259 EISELEKRLE------EIEQLLEEL----NKKIKDLGEEEQLRV-----------KEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   133 EAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQEL 212
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----------EEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   213 KHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLsrsSALHSDHAERDQEIHRLKMGMETLRVAN 292
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI---NELEEEKEDKALEIKKQEWKLEQLAADL 464

                          250
                   ....*....|....*..
gi 213972596   293 EDKDRRIEELTGLLNQY 309
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRV 481
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 715-784 4.89e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.37  E-value: 4.89e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   715 VVQWSNHRVMEWLRSVDLAEYAPNLRGSGVHGGLIILEprftgDTLAMLLNIPPQKTLLRRHLTTKFNAL 784
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 635-690 4.94e-08

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.37  E-value: 4.94e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596   635 VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTV-NDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKL 65
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 ...
 555-619 5.50e-08

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: 50.64  E-value: 5.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596 555 FAQWSTERVCTWLQDF-GL-AQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAI 619
Cdd:cd09562    1 FALWNGPTVVAWLELWvGMpAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
206-317 7.38e-08

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 56.02  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 206 EELLQELKHLKIKVEELEnernqyewelkatkAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGM 285
Cdd:COG2433  409 TEEEEEIRRLEEQVERLE--------------AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREI 474

                         90       100       110
                 ....*....|....*....|....*....|..
gi 213972596 286 ETLRVANEDKDRRIEELTGLLNQYLRVKEIVM 317
Cdd:COG2433  475 ERLERELEEERERIEELKRKLERLKELWKLEH 506
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 72-281 1.14e-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: 54.77  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  72 ALLSQIPGPTAAYIKEWFEDSLSQVNHHSAASnetyQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQV 151
Cdd:COG4942    8 ALLLALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 152 KLNAAEEMLQQellSRTSLETQKLDL---------MTEVSELKLKL---------VGMEKEQKEQEEKQRKAEELLQELK 213
Cdd:COG4942   84 ELAELEKEIAE---LRAELEAQKEELaellralyrLGRQPPLALLLspedfldavRRLQYLKYLAPARREQAEELRADLA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 214 HLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS----RSSALHSDHAERDQEIHRL 281
Cdd:COG4942  161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAelaaELAELQQEAEELEALIARL 232
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 558-627 2.26e-07

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: 48.85  E-value: 2.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 558 WSTERVCTWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAVKAinTKQEEKS 627
Cdd:cd09505    5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEE--LKMKSDS 72
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 107-336 2.76e-07

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 53.22  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  107 YQERLARLEGDKESLIlqvSVLTDQVEAQGekirdlevcLEGHQVKLNAAEEMLQQELLSRTslETQKLdlMTEVSELKL 186
Cdd:pfam09787  12 YKQKAARILQSKEKLI---ASLKEGSGVEG---------LDSSTALTLELEELRQERDLLRE--EIQKL--RGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  187 KLVGMEKEQKEQEEKQRKAEELLQE-LKHLKIKVEELENERNQYEWELKATKAEV----AQLQEQVALKDAEIERLHSQL 261
Cdd:pfam09787  76 ELQELEAQQQEEAESSREQLQELEEqLATERSARREAEAELERLQEELRYLEEELrrskATLQSRIKDREAEIEKLRNQL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596  262 SRSSALHSDHAERDQEIHRLkmgMETLRvaneDKDRRIEELT----GLLNQYLRVKEIVMATQGSSERTLSINEDEIEG 336
Cdd:pfam09787 156 TSKSQSSSSQSELENRLHQL---TETLI----QKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSINMEGISD 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
50-260 3.93e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   50 VLHLIEDLRLALEMLALPQEREALLSQIPGPTAAYIKEW-----FEDSLSQVNH-HSAASNETYQERLARLEGDKESLIL 123
Cdd:COG4913   230 LVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARerlaeLEYLRAALRLwFAQRRLELLEAELEELRAELARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  124 QVSVLTDQVEAQGEKIRDLEVCLEGHQV-KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqkeqeekq 202
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS----------- 378

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 213972596  203 rkAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4913   379 --AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-308 6.22e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 6.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  99 HSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEvcleghqVKLNAAEEMLQQELLSRTSLETQKLDLM 178
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEAEAELAEAE 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 179 TEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA-TKAEVAQLQEQVALKDAEIERL 257
Cdd:COG1196  379 EELEELAEEL----------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEElEEALAELEEEEEEEEEALEEAA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 213972596 258 HSQLSRSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQ 308
Cdd:COG1196  449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-383 7.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   108 QERLARLEGDKESLILQVSVLTDQVEaQGEKIRDLEVCLEGHQVKLNAAEemLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 LvgmekeqkeqeekqRKAEELLQELKHlkiKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSA- 266
Cdd:TIGR02168  262 L--------------QELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAq 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   267 ------------------------LHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGS 322
Cdd:TIGR02168  325 leeleskldelaeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596   323 SERTLSINEDEIEGSFRKWNTTSKSPEEVMKQEVSPRCSSPTPGPPPLPQKSLETRAQKKL 383
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-302 1.25e-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: 52.37  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 LVGMEKEQKEQEEKQRKAEELLQ-----------ELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIER 256
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 213972596   257 LHSQLSRSSA----LHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEEL 302
Cdd:TIGR02168  857 LAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSEELREL 906
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 54-286 2.47e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    54 IEDLRLALEMLalpQEREALLSQIPGPTAAYIKEwfedsLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTD--- 130
Cdd:TIGR02169  718 IGEIEKEIEQL---EQEEEKLKERLEELEEDLSS-----LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArls 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   131 -----QVEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVgmeKEQKEQEEKQRKA 205
Cdd:TIGR02169  790 hsripEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNGKK 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   206 EELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGM 285
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943


                   .
gi 213972596   286 E 286
Cdd:TIGR02169  944 E 944
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 109-359 2.65e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 51.51  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   109 ERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQ-VKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLK 187
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 lvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEwelKATKAEVAQLQEQVALKDAEIERLHSQLSRSSAL 267
Cdd:pfam02463  323 ---KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   268 HS----DHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRKWNT 343
Cdd:pfam02463  397 LElkseEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476

                          250
                   ....*....|....*.
gi 213972596   344 TSKSPEEVMKQEVSPR 359
Cdd:pfam02463  477 TQLVKLQEQLELLLSR 492
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
558-619 2.68e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 2.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596  558 WSTERVCTWLQDFGLAQYV-IFARQWVASGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 619
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTdNFRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 556-616 2.95e-06

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: 45.52  E-value: 2.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 556 AQWSTERVCTWLQ-DFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 616
Cdd:cd09564    2 SRWKADMVLAWLEvVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAI 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-260 6.56e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  65 ALPQEREALLSQIPGPTAAYIKEWfeDSLSQVNHHSAASNETY---QERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:COG4717   50 RLEKEADELFKPQGRKPELNLKEL--KELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 142 LEVCLEGHQVKLNAAE-----EMLQQELLSRTSLETQKLDLMTEVSELKLKLVgmekeqkeqEEKQRKAEELLQELKHLK 216
Cdd:COG4717  128 LPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQEELE---------ELLEQLSLATEEELQDLA 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 213972596 217 IKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQ 260
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 558-614 6.91e-06

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 44.63  E-value: 6.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596 558 WSTERVCTWLQDF-GLAQYVIFARQWVASGHTL---LTATPQDMEKELGIKHPLHRKKLVL 614
Cdd:cd09504    5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALprlAVNNPSFLTSVLGIKDPIHRQKLSL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-354 7.16e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 7.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 163 ELLSRTSLETQKLDlmTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKiKVEELENERNQYEWE-LKATKAEVA 241
Cdd:PRK03918 452 ELLEEYTAELKRIE--KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEeLEKKAEEYE 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 242 QLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLK------------MGMETLrvanEDKDRRIEELTGLLNQY 309
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEeelaellkeleeLGFESV----EELEERLKELEPFYNEY 604

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 213972596 310 LRVKEIVMATQgSSERTLSINEDEIEGSFRKWNTTSKSPEEVMKQ 354
Cdd:PRK03918 605 LELKDAEKELE-REEKELKKLEEELDKAFEELAETEKRLEELRKE 648
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
632-687 7.88e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.18  E-value: 7.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596  632 HVW----VTRWLDDIGLPQYKDQFYESRVDG-RMLQYLTVNDLLFLKVTSQLHHLSIKCAI 687
Cdd:pfam07647   2 ESWslesVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI 62
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 632-690 8.00e-06

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: 44.23  E-value: 8.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 632 HVW----VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09506    3 HEWtvddVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 635-690 2.00e-05

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) subfamily is a putative protein-protein interaction domain. SAM is widespread domain in proteins involved in signal transduction and regulation. In many cases SAM mediates homodimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188929  Cd Length: 67  Bit Score: 43.08  E-value: 2.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972596 635 VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09530    8 VAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 563-616 2.09e-05

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: 43.17  E-value: 2.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 213972596 563 VC-TWLQDFGLAQYVIFARQWVASGHTLLTATPQDMEKELGIKHPLHRKKLVLAV 616
Cdd:cd09567    7 VArEWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGI 61
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-307 2.14e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  104 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLE---VCLEGHQVKLNAAEEMLQQEL--LSRtSLETQKLDLM 178
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  179 TEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEV---------AQLQEQVAL 249
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDE 565

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 213972596  250 KDAEIERLHSQlsrSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLN 307
Cdd:TIGR04523 566 KNKEIEELKQT---QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 554-617 3.48e-05

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 42.40  E-value: 3.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972596 554 PFAQWSTERVCTWLQDFGLAQYV-IFARQWVaSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVK 617
Cdd:cd09507    1 PVTNWTTEEVGAWLESLQLGEYRdIFARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIK 63
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 559-612 5.02e-05

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 41.86  E-value: 5.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596 559 STERVCTWLQDFGLAQYvifARQWVASGHTLLT---ATPQDMeKELGIKHPLHRKKL 612
Cdd:cd09497    3 DAEAIFDWLREFGLEEY---TPNFIKAGYDLPTisrMTPEDL-TAIGITKPGHRKKL 55
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 105-266 5.26e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 105 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQ---------------------- 162
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgse 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 163 ---ELLSRTS----LETQKLDLMTEVSELKLKLvgmekeQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKA 235
Cdd:COG3883  113 sfsDFLDRLSalskIADADADLLEELKADKAEL------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                        170       180       190
                 ....*....|....*....|....*....|.
gi 213972596 236 TKAEVAQLQEQVALKDAEIERLHSQLSRSSA 266
Cdd:COG3883  187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 635-688 5.55e-05

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 41.53  E-value: 5.55e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 213972596 635 VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIH 688
Cdd:cd09533    2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVY 55
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 69-316 5.58e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.04  E-value: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    69 EREALLSQIPGPTAAY--IKEWFEDSLSQVNHHSAASNETYQERlARLE---GDKESLILQVSVLTDQVEAqgeKIRDLE 143
Cdd:pfam15921  549 ECEALKLQMAEKDKVIeiLRQQIENMTQLVGQHGRTAGAMQVEK-AQLEkeiNDRRLELQEFKILKDKKDA---KIRELE 624

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   144 VC---LEGHQVKL-NAAEEMLQqellSRTSLETQKLDLMTEVSELKLKLVGMEKEQkeqeekqrkaeELLQelKHLKIKV 219
Cdd:pfam15921  625 ARvsdLELEKVKLvNAGSERLR----AVKDIKQERDQLLNEVKTSRNELNSLSEDY-----------EVLK--RNFRNKS 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   220 EELENERNQYEWELKATKAEVAQ---------------------LQEQVALKDAEIERLHSQLsrsSALHSDHAERDQEI 278
Cdd:pfam15921  688 EEMETTTNKLKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKI---QFLEEAMTNANKEK 764

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 213972596   279 HRL-----KMGMETLRVANEdKDRRIEELTGLLNQYLRVKEIV 316
Cdd:pfam15921  765 HFLkeeknKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKV 806
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 632-688 8.42e-05

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 41.55  E-value: 8.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 632 HVW----VTRWL-DDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLkvTSQlhhLSIKCAIH 688
Cdd:cd09504    3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALPRLAVNNPSFL--TSV---LGIKDPIH 59
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
65-301 1.00e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  65 ALPQEREALLSQipgptaayiKEWFEDSLSQVNHHSAASN---ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRD 141
Cdd:PRK02224 311 AVEARREELEDR---------DEELRDRLEECRVAAQAHNeeaESLREDADDLEERAEELREEAAELESELEEAREAVED 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 142 LEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELL---------QEL 212
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPV 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 213 KHLKI---------KVEELENERNQYEWELKATKAEVAQLQEQVALKDaEIERLHSQLSRSSALHSDHAERDQEiHRLKm 283
Cdd:PRK02224 462 EGSPHvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEE-KRER- 538

                        250
                 ....*....|....*...
gi 213972596 284 gMETLRVANEDKDRRIEE 301
Cdd:PRK02224 539 -AEELRERAAELEAEAEE 555
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
104-263 1.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 104 NETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSE 183
Cdd:COG4372    5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 184 LKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR 263
Cdd:COG4372   85 LNEQL---QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-303 1.31e-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: 45.83  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   130 DQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqELLSRTSLETQKL-DLMTEVSELKlklvgmekeqkeqeekqRKAEEL 208
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIgEIEKEIEQLE-----------------QEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   209 LQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS---------SALHSDHA------- 272
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelSKLEEEVSriearlr 815

                          170       180       190
                   ....*....|....*....|....*....|.
gi 213972596   273 ERDQEIHRLKMGMETLRVANEDKDRRIEELT 303
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 556-617 1.49e-04

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: 40.70  E-value: 1.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972596 556 AQWSTERVCTWLQDFGLAQYV-IFARQWVASGHTLLTATPQDM-EKELGIKHPLHRKKLVLAVK 617
Cdd:cd09515    2 HEWTCEDVAKWLKKEGFSKYVdLLCNKHRIDGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIR 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-249 1.64e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    53 LIEDLRLALEMLalpQEREALLSQIPGPTAAYIKEWFEDSLsqvnhHSAASNETYQERLARLEGDKESLILQVSVLTDQV 132
Cdd:TIGR02168  296 EISRLEQQKQIL---RERLANLERQLEELEAQLEELESKLD-----ELAEELAELEEKLEELKEELESLEAELEELEAEL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   133 EAQGEKIRDLEVCLEG---------HQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQR 203
Cdd:TIGR02168  368 EELESRLEELEEQLETlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 213972596   204 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVAL 249
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 105-354 2.53e-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: 44.71  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  105 ETYQERLarleGDKESlilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE--MLQQELLSRtsLETQKLDLMTEVS 182
Cdd:pfam05483 229 EEYKKEI----NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELE 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  183 ELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLK-IKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 261
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  262 SRSSALHSDHAERDQEIHRLKMGMEtlrVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSER---TLSINEDEIEGSF 338
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKE---VELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQElifLLQAREKEIHDLE 456

                         250
                  ....*....|....*.
gi 213972596  339 RKWNTTSKSPEEVMKQ 354
Cdd:pfam05483 457 IQLTAIKTSEEHYLKE 472
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-311 2.85e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  91 DSLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEghQVKLNAAEEMLQQeLLSRTSL 170
Cdd:COG4717  305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAA-LLAEAGV 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 171 ET------------QKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKaEELLQELKHLKIKVEELENERNQYEWELKATKA 238
Cdd:COG4717  382 EDeeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEA 460

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213972596 239 EVAQLQEQVAL--KDAEIERLHSQLsrssalhsdhAERDQEIHRLKMGMETL-RVANEDKDRRIEELTGLLNQYLR 311
Cdd:COG4717  461 ELEQLEEDGELaeLLQELEELKAEL----------RELAEEWAALKLALELLeEAREEYREERLPPVLERASEYFS 526
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
203-341 5.32e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 203 RKAEELLQELKHLKIKVEELENERNQY---EWELKATKAEVAQLQEQVALKDAEIERLHSQLsrssalhsDHAERDQEIH 279
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLL--------QLLPLYQELE 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972596 280 RLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRKW 341
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
PTZ00121 PTZ00121
MAEBL; Provisional
 135-340 5.58e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  135 QGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKeqeEKQRKAEELLQELKH 214
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  215 LKIKVEEL----ENERNQYEwELKATKAEVAQLQEQVAlKDAEIERLHSQLSRSSALHSDHAE---RDQEIHRLKmgMET 287
Cdd:PTZ00121 1659 NKIKAAEEakkaEEDKKKAE-EAKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIK--AEE 1734

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 213972596  288 LRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRK 340
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 635-669 7.20e-04

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 38.77  E-value: 7.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 213972596 635 VTRWLDDIGLPQYKDQF-YESRVDGRMLQYLTVNDL 669
Cdd:cd09515    9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 552-603 7.46e-04

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 38.79  E-value: 7.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 213972596 552 NAPFAQWSTERVCTWLQDFGLAQYV-IFARQWVaSGHTLLTATPQDMeKELGI 603
Cdd:cd09512    1 SRPVSEWSVQQVCQWLMGLGLEQYIpEFTANNI-DGQQLLQLDSSKL-KALGI 51
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 556-604 7.83e-04

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 38.81  E-value: 7.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 213972596 556 AQWSTERVCTWLQ--DFGLAQYVIFARQWVASGHTLLTATPQDMEkELGIK 604
Cdd:cd09511    2 AKWSPKQVTDWLKglDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 204-263 8.14e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 8.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 204 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSR 263
Cdd:COG3883   31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-311 9.48e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  108 QERLARLEGdkeslilQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQqelLSRTSLETQKLDlmTEVSELKLK 187
Cdd:COG4913   609 RAKLAALEA-------ELAELEEELAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDVASAE--REIAELEAE 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  188 LvgmekeqkeqeekqRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSAL 267
Cdd:COG4913   677 L--------------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972596  268 HSDHAERDQEIHRLKMGMET------------LRVANEDKDRRIEELTGLLNQYLR 311
Cdd:COG4913   743 ARLELRALLEERFAAALGDAverelrenleerIDALRARLNRAEEELERAMRAFNR 798
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 110-161 9.96e-04

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


Pssm-ID: 396208 [Multi-domain]  Cd Length: 95  Bit Score: 39.04  E-value: 9.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 213972596  110 RLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQ 161
Cdd:pfam01519  26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 118-351 1.22e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.50  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  118 KESLILQ---VSVLTDQVEAqgekirdLEVCLEGHQVKLNAAEEMLQ--QELLSRTSLETQKLDLMTEVSELKLKLVgme 192
Cdd:pfam10174 330 KESLTAKeqrAAILQTEVDA-------LRLRLEEKESFLNKKTKQLQdlTEEKSTLAGEIRDLKDMLDVKERKINVL--- 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  193 keqkeqeekQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRS-------- 264
Cdd:pfam10174 400 ---------QKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdrerleel 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  265 --------------SALHSDHAERDQEIHRLKMGMETLRVANEDKDRRI-----------EELTGLLNQYLRVKEIVMAT 319
Cdd:pfam10174 471 eslkkenkdlkekvSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiaveqkkEECSKLENQLKKAHNAEEAV 550

                         250       260       270
                  ....*....|....*....|....*....|..
gi 213972596  320 QGSSERTLSINEDEIEGSFRKwNTTSKSPEEV 351
Cdd:pfam10174 551 RTNPEINDRIRLLEQEVARYK-EESGKAQAEV 581
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 565-620 1.25e-03

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 38.04  E-value: 1.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596 565 TWLQDFGLAQYV-IFARQWVASGHTLLTATPQDMEkELGIKHPLHRKKLVLAVKAIN 620
Cdd:cd09498   12 EWLSLLGLPQYHkVLVENGYDSIDFVTDLTWEDLQ-DIGITKLGHQKKLMLAIKKLK 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
203-350 1.29e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 203 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDhAERDQEIHRlk 282
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSE-- 300

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213972596 283 mgmetLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGSFRKWNTTSKSPEE 350
Cdd:PRK03918 301 -----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 105-301 1.45e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  105 ETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLevcleghqvklnaaeemlqQELLSRTslETQKLDLMTEVSEL 184
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------------------TTEISNT--QTQLNQLKDEQNKI 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  185 KLKLvgmekeqkeqeekqrkaEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQ-----LQEQVALKDAEIERLHS 259
Cdd:TIGR04523 266 KKQL-----------------SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQN 328

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 213972596  260 QLSRSSALHSdhaERDQEIHRLKMGMETLRVANEDKDRRIEE 301
Cdd:TIGR04523 329 QISQNNKIIS---QLNEQISQLKKELTNSESENSEKQRELEE 367
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
68-355 1.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  68 QEREALLSQIPGpTAAYIKEWfeDSLSQVNHHSAASNETYQERLARlEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLE 147
Cdd:PRK03918 145 ESREKVVRQILG-LDDYENAY--KNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELR 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 148 GHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEE---LEN 224
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikLSE 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 225 ERNQYEWELKATKAEVAQLQEQValkdAEIERLHSQLSrssalhsdhaERDQEIHRLKMGMETLRvanedkdRRIEELTG 304
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEI----NGIEERIKELE----------EKEERLEELKKKLKELE-------KRLEELEE 359

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 213972596 305 LLNQYLRVKEIVMATQGSSERTLSINEDEIEgsfRKWNTTSKSPEEVMKQE 355
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEI 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 204-311 1.76e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   204 KAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKM 283
Cdd:TIGR02168  692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100
                   ....*....|....*....|....*...
gi 213972596   284 GMETLRVANEDKdrrIEELTGLLNQYLR 311
Cdd:TIGR02168  772 EAEEELAEAEAE---IEELEAQIEQLKE 796
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 89-282 1.76e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.04  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   89 FEDSLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQvEAQGEKIRDLEVCLEGhqvKLNAAEEMLQQELLSRT 168
Cdd:pfam05557  53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK-ESQLADAREVISCLKN---ELSELRRQIQRAELELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  169 SLETQKLDLMTEVSELKLKLVGMEKEQKEQeekqrkaEELLQELKHLKIKVEELENERNQYE-W--ELKATKAEVAQLQE 245
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNL-------EKQQSSLAEAEQRIKELEFEIQSQEqDseIVKNSKSELARIPE 201

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 213972596  246 QvalkDAEIERLHSQLSRSSALHSDHAERDQEIHRLK 282
Cdd:pfam05557 202 L----EKELERLREHNKHLNENIENKLLLKEEVEDLK 234
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 113-361 1.91e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   113 RLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 192
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   193 KEQKEQEEKQRKAEEllqELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDA--------------EIERLH 258
Cdd:pfam01576  229 AQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrdlgeELEALK 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   259 SQLSRS----SALHSDHAERDQEIHRLKMGMETLRVANEDK--DRR------IEELTGLLNQYLRVKEIVMATQGSSE-- 324
Cdd:pfam01576  306 TELEDTldttAAQQELRSKREQEVTELKKALEEETRSHEAQlqEMRqkhtqaLEELTEQLEQAKRNKANLEKAKQALEse 385

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 213972596   325 --------RTLSINEDEIEGSFRKwnttskspEEVMKQEVSPRCS 361
Cdd:pfam01576  386 naelqaelRTLQQAKQDSEHKRKK--------LEGQLQELQARLS 422
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 558-612 2.01e-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: 37.67  E-value: 2.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972596 558 WSTERVCTWLQDFGLAQYV-IFARQWVaSGHTLLTATPQDMEKELGIKHPLHRKKL 612
Cdd:cd09501    4 WSVADVQTWLKQIGFEDYAeKFSESQV-DGDLLLQLTEDELKQDLGMSSGLLRKRF 58
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-276 2.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 109 ERLARLEGDKESLILQVSV---LTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQE--LLSRTSLETQKLDLMTEVSE 183
Cdd:COG4717   71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLplYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 184 LKLKLvgmekeqKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEW--------ELKATKAEVAQLQEQVALKDAEIE 255
Cdd:COG4717  151 LEERL-------EELRELEEELEELEAELAELQEELEELLEQLSLATEeelqdlaeELEELQQRLAELEEELEEAQEELE 223

                        170       180
                 ....*....|....*....|.
gi 213972596 256 RLHSQLSRSSALHSDHAERDQ 276
Cdd:COG4717  224 ELEEELEQLENELEAAALEER 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-302 2.67e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEMLQQELLSRTSLETQkldlmteVSELKLK 187
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA-------LALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   188 LVGMEKEQKEQEEKQRKAEELLQELKHlkikveelenERNQYEWELKATKAEVAQLQEQVAlKDAEIErLHSQLSRSSAL 267
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELRE----------KLAQLELRLEGLEVRIDNLQERLS-EEYSLT-LEEAEALENKI 963

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 213972596   268 HSDHAERDQEIHRLKMGMETLRVANEDKdrrIEEL 302
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKIKELGPVNLAA---IEEY 995
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 85-307 2.93e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   85 IKEWFEDSLSQVNHHSAASNE------TYQERLARLEGDKESLILqvSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE 158
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKElekqlnQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  159 MLQQELLSRTSLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKA 238
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEI----------EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596  239 EVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAErdqEIHRLKMGMETLRVANEDKDRRIEELTGLLN 307
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN---QDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 203-266 3.20e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972596 203 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSA 266
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 108-337 3.25e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVklnaaeemlqqellsrtsleTQKLDLMTEVSELKlk 187
Cdd:COG5185  274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQ--------------------LAAAEAEQELEESK-- 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 188 lvgmekeqkeqeekqRKAEELLQELKHlkikveELENERNQYEWELKATKAEVAQLQEQVALKDAEiERLHS-QLSRSSA 266
Cdd:COG5185  332 ---------------RETETGIQNLTA------EIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSfKDTIEST 389

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596 267 LHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIEGS 337
Cdd:COG5185  390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEE 460
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-246 3.53e-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: 39.91  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 108 QERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEEM------------LQQEL----LSRTSLE 171
Cdd:COG1579   30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972596 172 TQKLDLMTEVSELKLKLvgmekeqkeqeekqrkaEELLQELKHLKIKVEELENERNQyewELKATKAEVAQLQEQ 246
Cdd:COG1579  110 DEILELMERIEELEEEL-----------------AELEAELAELEAELEEKKAELDE---ELAELEAELEELEAE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-335 3.74e-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: 40.52  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 203 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERD------- 275
Cdd:COG4942   48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplallls 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596 276 -QEIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIE 335
Cdd:COG4942  128 pEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 632-690 4.55e-03

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.47  E-value: 4.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596 632 HVW----VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDLLFLKVTSQLHHLSIKCAIHVL 690
Cdd:cd09575    3 HLWgteeVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 554-619 4.64e-03

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


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.47  E-value: 4.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972596 554 PFAQWSTERVCTWLQDFGLAQYV-IFARQWVaSGHTLLTATPQDMeKELGIKHPLHRKKLVLAVKAI 619
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLSLCEYKdIFTRHDV-RGSELLHLERRDL-KDLGVTKVGHMKRILCGIKEL 65
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 54-328 4.77e-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: 40.87  E-value: 4.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    54 IEDLR-LALEMLALPQEREALLSQIPGPTAAYIKEwfEDSLSQVNHHSAASneTYQERLARLEGDKESLILQVSVLTDQV 132
Cdd:pfam15921  172 IEQLRkMMLSHEGVLQEIRSILVDFEEASGKKIYE--HDSMSTMHFRSLGS--AISKILRELDTEISYLKGRIFPVEDQL 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   133 EA-QGEKIRDLEVCLEGHQVKL-------------------------NAAE---EMLQQELLSRTSLETQKL-DLMTEVS 182
Cdd:pfam15921  248 EAlKSESQNKIELLLQQHQDRIeqliseheveitgltekassarsqaNSIQsqlEIIQEQARNQNSMYMRQLsDLESTVS 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   183 ELKLKLvgmekeqkeqeekqRKAEELLQElkhlkiKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLS 262
Cdd:pfam15921  328 QLRSEL--------------REAKRMYED------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   263 RSSALHSDHAERDQEIHRLKMG----METLRVANEDKDRRIEELTGLLnqylrvKEIVMATQGSSERTLS 328
Cdd:pfam15921  388 KREKELSLEKEQNKRLWDRDTGnsitIDHLRRELDDRNMEVQRLEALL------KAMKSECQGQMERQMA 451
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 58-267 5.37e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    58 RLALEMLALPQEREALLSQIPGPTAAYIKEWFEDSLSQVNhhsaASNETYQERLARLEGDKESLILQVSVLTDQVEAQGE 137
Cdd:TIGR00618  640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ----LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   138 KIRDL-EVCLEGH--QVKLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGMekeqkeqeekqrkAEELLQELKH 214
Cdd:TIGR00618  716 YDREFnEIENASSslGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA-------------ALQTGAELSH 782

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213972596   215 LKIKVEELENERNQYEWELKATKAEVAQ--------LQEQVALKDAEIERLHSQLSRSSAL 267
Cdd:TIGR00618  783 LAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSAT 843
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 85-299 5.78e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   85 IKEWFEDSLSQVNHHSAASNETYQERLarlegdKESLILQVSVLTDQV--------EAQGEKIRDLEVCLEGHQVKLNAA 156
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAVRT------NPEINDRIRLLEQEVarykeesgKAQAEVERLLGILREVENEKNDKD 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  157 EEMlqQELLSRTSLetQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQElKHLKIKVEELENERNQYEWELKAT 236
Cdd:pfam10174 600 KKI--AELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD-NSQQLQLEELMGALEKTRQELDAT 674

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972596  237 KAEVAQLQEQVALKDAEIERLHsqlsrssalhsdHAERDQEIHRLKMGMETLRVANEDKDRRI 299
Cdd:pfam10174 675 KARLSSTQQSLAEKDGHLTNLR------------AERRKQLEEILEMKQEALLAAISEKDANI 725
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 54-257 5.82e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596    54 IEDLRLALEMLalpqEREALLSQIPGPTAAY--IKEWFEDSLSQVNHHSAASNETYQERlARLEGDKESLILQVSVLTDQ 131
Cdd:TIGR02169  774 LHKLEEALNDL----EARLSHSRIPEIQAELskLEEEVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQ 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   132 VEAQGEKIRDLEVCLEghqvKLNAAEEMLQQELLSrtsLETQKLDLMTEVSELKLKLvgmekeqkeqEEKQRKAEEL--- 208
Cdd:TIGR02169  849 IKSIEKEIENLNGKKE----ELEEELEELEAALRD---LESRLGDLKKERDELEAQL----------RELERKIEELeaq 911

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596   209 LQELKH----LKIKVEELENERNQYEWELKATKAEVA------QLQEQVALKDAEIERL 257
Cdd:TIGR02169  912 IEKKRKrlseLKAKLEALEEELSEIEDPKGEDEEIPEeelsleDVQAELQRVEEEIRAL 970
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 92-245 5.98e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.43  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   92 SLSQVNHHSAASNETYQERLARLEGDKESLILQVSVLTDQVEAQGEKIRDLEVCLEGHQVKLNAAEE---MLQQEL---- 164
Cdd:pfam05911 671 LVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKEsnsLAETQLkcma 750

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  165 LSRTSLETQKLDLMTEVSELKLKlvgMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERN------------QYEWE 232
Cdd:pfam05911 751 ESYEDLETRLTELEAELNELRQK---FEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESsncdadqedkklQQEKE 827

                         170
                  ....*....|...
gi 213972596  233 LKATKAEVAQLQE 245
Cdd:pfam05911 828 ITAASEKLAECQE 840
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 203-261 6.05e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 6.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596  203 RKAEELLQELKHLKIKVEElenERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL 261
Cdd:pfam20492  58 QEAEEEKERLEESAEMEAE---EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
COG5022 COG5022
Myosin heavy chain [General function prediction only];
94-425 6.05e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   94 SQVNHHSAASNETYQERLARLEgdKESLILQVSVLTDQVEAQ--GEKIRDLEV--------CLEGHQVKLN---AAEEML 160
Cdd:COG5022   844 AEVLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQlqELKIDVKSIsslklvnlELESEIIELKkslSSDLIE 921

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  161 QQELLSRTSLETQKLDLMTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEV 240
Cdd:COG5022   922 NLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL 1001

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  241 AQLQEQVALKDAEIERLHSQLSRSSALHSDhaerdqeIHRLKMGMETLRVANEdkdrrIEELTGLL---NQYLRVKEIVM 317
Cdd:COG5022  1002 AELSKQYGALQESTKQLKELPVEVAELQSA-------SKIISSESTELSILKP-----LQKLKGLLlleNNQLQARYKAL 1069

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  318 ATQGSSERTLSINEDEIEGSFRKWNTTSKSPEEVMKQEVSPrcSSPTPGPPPLPQKSLETRAQKKLSCSLEDLRCESGNK 397
Cdd:COG5022  1070 KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVK--PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQ 1147

                         330       340
                  ....*....|....*....|....*...
gi 213972596  398 CINGNQTSPVGEPKDSSFlaEQKYPTLP 425
Cdd:COG5022  1148 KLSVLQLELDGLFWEANL--EALPSPPP 1173
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-353 6.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  98 HHSAASNETYQERLARLEGDKESLilqvsvltdqveaqGEKIRDLEVCLEGHQVKLNAAEEMLQQ----ELLSRTSLETQ 173
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEI--------------EEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLK 513

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 174 KLDL------MTEVSELKLKLVGMEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAqlqEQV 247
Cdd:PRK03918 514 KYNLeelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EEL 590

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 248 ALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLKMGMETLRVANEDKDRRIEELTGLLNQyLRVKEIVMATQGSSERTL 327
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELREEYL 669

                        250       260
                 ....*....|....*....|....*.
gi 213972596 328 SInEDEIEGSFRKWNTTSKSPEEVMK 353
Cdd:PRK03918 670 EL-SRELAGLRAELEELEKRREEIKK 694
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-335 6.56e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   203 RKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQLSRSSALHSDHAERDQEIHRLk 282
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE- 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 213972596   283 mgMETLRVANEDKDRRIEELTGLLNQYLRVKEIVMATQGSSERTLSINEDEIE 335
Cdd:TIGR02168  756 --LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
155-289 6.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596 155 AAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLvgmEKEQKEQEEKQRKAEELLQELKHLKIKVEELENERNQYEWELK 234
Cdd:COG4372   28 ALSEQLRKALFELDKLQEELEQLREELEQAREEL---EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213972596 235 ATKAEVAQLQEQVALKDAEIERLHSQLSR----SSALHSDHAERDQEIHRLKMGMETLR 289
Cdd:COG4372  105 SLQEEAEELQEELEELQKERQDLEQQRKQleaqIAELQSEIAEREEELKELEEQLESLQ 163
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 62-315 8.45e-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: 39.70  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596   62 EMLALPQEREALLSQIPGPTAAyiKEWFEDSLSQVNHHSAASNETYQERLARLEG-DKE--SLILQVSVLTDQVEAQGEK 138
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIAEELKGKEQELIFLLQArEKEihDLEIQLTAIKTSEEHYLKE 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  139 IRDLEVCLEGHQVK---LNAAEEML---QQELLSRTS-----LETQKLDLMT--EVSELKLKLVGMEKEQKEQEEKQRKA 205
Cdd:pfam05483 473 VEDLKTELEKEKLKnieLTAHCDKLlleNKELTQEASdmtleLKKHQEDIINckKQEERMLKQIENLEEKEMNLRDELES 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  206 --EELLQELKHLKIKVEELENERNQYEWE-------LKATKAEVAQLQEQVALKDAEIERLHSQlsrSSALHSDHAERDQ 276
Cdd:pfam05483 553 vrEEFIQKGDEVKCKLDKSEENARSIEYEvlkkekqMKILENKCNNLKKQIENKNKNIEELHQE---NKALKKKGSAENK 629

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 213972596  277 EIHRLKMGMETLRVANEDKDRRIEELTGLLNQYLRVKEI 315
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI 668
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 635-669 8.64e-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: 35.74  E-value: 8.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 213972596 635 VTRWLDDIGLPQYKDQFYESRVDGRMLQYLTVNDL 669
Cdd:cd09501    9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDEL 43
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
124-305 9.62e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  124 QVSVLT------DQVEAQGEKIRDLEVCLEGHQV-----KLNAAEEMLQQELLSRTSLETQKLDLMTEVSELKLKLVGME 192
Cdd:COG4913   250 QIELLEpirelaERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972596  193 KeqkeqeekqRKAEELLQELKHLKIKVEELENERNQYEWELKATKAEVAQLQEQVALKDAEIERLHSQL-SRSSALHSDH 271
Cdd:COG4913   330 A---------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAaALLEALEEEL 400

                         170       180       190
                  ....*....|....*....|....*....|....
gi 213972596  272 AERDQEIHRLKmgmETLRVANEDKDRRIEELTGL 305
Cdd:COG4913   401 EALEEALAEAE---AALRDLRRELRELEAEIASL 431
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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