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Conserved domains on  [gi|2462535240|ref|XP_054229613|]
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liprin-beta-1 isoform X31 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 675-746 2.97e-46

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


:

Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.54  E-value: 2.97e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 675 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 746
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 ...
 590-652 3.82e-38

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


:

Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 3.82e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 590 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
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 ...
 516-579 5.12e-34

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


:

Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.26  E-value: 5.12e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535240 516 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 579
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-216 2.28e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    2 LQQEL--LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTK 79
Cdd:TIGR02168  218 LKAELreLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   80 SLMAKLSSMK-----------IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDR 148
Cdd:TIGR02168  295 NEISRLEQQKqilrerlanleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESR 373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240  149 DENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRykkmQDTVVLAQGKKGKDGEYEE 216
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKE 437
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
 110-374 3.37e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  110 KDELASLKEQLEEKESEVKRLQEKLVCKM-------------KGEGVEIVDRDE----NFKKKLKEKNIEVQKMKKAVES 172
Cdd:PTZ00108  1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMwledldkfeealeEQEEVEEKEIAKeqrlKSKTKGKASKLRKPKLKKKEKK 1180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  173 LMAANEEKDRKIEDLRqclnRYKKMQDTVVLAQGKKGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPScdp 252
Cdd:PTZ00108  1181 KKKSSADKSKKASVVG----NSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKS--- 1253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  253 fntsvPEEFHTTILQVSIPSLLPATVSMETSEKSKLTPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNL 331
Cdd:PTZ00108  1254 -----SEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462535240  332 KKETSDGEKetiqKTSEDRAPAESRPFGTLPPRPPGQDTSMDD 374
Cdd:PTZ00108  1329 KKTARKKKS----KTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
 
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 ...
 675-746 2.97e-46

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.54  E-value: 2.97e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 675 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 746
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 ...
 590-652 3.82e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 3.82e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 590 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
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 ...
 516-579 5.12e-34

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.26  E-value: 5.12e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535240 516 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 579
Cdd:cd09563     1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 592-652 2.03e-18

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 80.01  E-value: 2.03e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 592 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 518-580 8.90e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 8.90e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 518 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 580
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 516-580 3.98e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.31  E-value: 3.98e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240  516 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 580
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 592-652 1.23e-11

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 60.77  E-value: 1.23e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240  592 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
679-746 4.25e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.25e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 679 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 746
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-216 2.28e-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: 64.69  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    2 LQQEL--LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTK 79
Cdd:TIGR02168  218 LKAELreLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   80 SLMAKLSSMK-----------IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDR 148
Cdd:TIGR02168  295 NEISRLEQQKqilrerlanleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESR 373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240  149 DENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRykkmQDTVVLAQGKKGKDGEYEE 216
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKE 437
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
20-196 8.92e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  20 MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKkLKSTKSLMAKLSSMKIKVGQMQYEK 99
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 100 QRMEQKWEslkdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE 179
Cdd:COG4717   149 EELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                         170
                  ....*....|....*..
gi 2462535240 180 KDRKIEDLRQCLNRYKK 196
Cdd:COG4717   225 LEEELEQLENELEAAAL 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-196 1.14e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  10 TSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLS 86
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  87 SmKIKvgqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKGEGVEIVDRDENFKKKLKEKNIEvqKM 166
Cdd:PRK03918  321 E-EIN------GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTPE--KL 389

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462535240 167 KKAVESLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKK 419
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 676-745 1.03e-06

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 46.91  E-value: 1.03e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  676 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 745
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 2-206 6.00e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.17  E-value: 6.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEindLRLKVSEMDSERLQYEKK------- 74
Cdd:pfam01576  365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE---LQARLSESERQRAELAEKlsklqse 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   75 LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWESLKDELASLKEQLEEkESEVKRLQEKLVC 136
Cdd:pfam01576  442 LESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQLS 520

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240  137 KMKGEGVEivdrdenFKKKLKEKNIEVQ-------KMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQG 206
Cdd:pfam01576  521 TLQAQLSD-------MKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 40-209 2.62e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   40 YEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSsmkikvgqmqyekqrmeQKWESLKDELASLKEQ 119
Cdd:smart00787 135 YEWRMKLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPKLR-----------------DRKDALEEELRQLKQL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  120 LEEKES----EVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR-Y 194
Cdd:smart00787 195 EDELEDcdptELDRAKEKLK-KLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKeI 273

                          170
                   ....*....|....*
gi 2462535240  195 KKMQDTVVLAQGKKG 209
Cdd:smart00787 274 EKLKEQLKLLQSLTG 288
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 110-374 3.37e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  110 KDELASLKEQLEEKESEVKRLQEKLVCKM-------------KGEGVEIVDRDE----NFKKKLKEKNIEVQKMKKAVES 172
Cdd:PTZ00108  1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMwledldkfeealeEQEEVEEKEIAKeqrlKSKTKGKASKLRKPKLKKKEKK 1180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  173 LMAANEEKDRKIEDLRqclnRYKKMQDTVVLAQGKKGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPScdp 252
Cdd:PTZ00108  1181 KKKSSADKSKKASVVG----NSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKS--- 1253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  253 fntsvPEEFHTTILQVSIPSLLPATVSMETSEKSKLTPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNL 331
Cdd:PTZ00108  1254 -----SEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462535240  332 KKETSDGEKetiqKTSEDRAPAESRPFGTLPPRPPGQDTSMDD 374
Cdd:PTZ00108  1329 KKTARKKKS----KTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
 
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 ...
 675-746 2.97e-46

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


Pssm-ID: 188968  Cd Length: 72  Bit Score: 159.54  E-value: 2.97e-46
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 675 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 746
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 ...
 590-652 3.82e-38

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


Pssm-ID: 188965  Cd Length: 63  Bit Score: 135.90  E-value: 3.82e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 590 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
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 ...
 516-579 5.12e-34

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 124.26  E-value: 5.12e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535240 516 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 579
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 ...
 683-744 1.76e-33

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


Pssm-ID: 188895  Cd Length: 62  Bit Score: 122.65  E-value: 1.76e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 683 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 744
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 ...
 679-746 1.99e-31

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 117.16  E-value: 1.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 679 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 746
Cdd:cd09570     5 WTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 595-652 1.56e-20

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


Pssm-ID: 188894  Cd Length: 60  Bit Score: 85.66  E-value: 1.56e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535240 595 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 652
Cdd:cd09495     2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 592-652 2.03e-18

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 80.01  E-value: 2.03e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 592 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:pfam00536   4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 679-746 4.18e-18

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 79.28  E-value: 4.18e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 679 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 746
Cdd:cd09568     5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 518-580 8.90e-15

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 8.90e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 518 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 580
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 524-579 3.58e-14

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 67.64  E-value: 3.58e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240 524 VCNWLMEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 579
Cdd:cd09494     2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 595-649 4.57e-13

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 64.57  E-value: 4.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240 595 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 649
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 590-652 8.23e-13

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 63.97  E-value: 8.23e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240 590 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 652
Cdd:cd09567     1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 516-580 3.98e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 62.31  E-value: 3.98e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240  516 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 580
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 592-652 1.23e-11

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 60.77  E-value: 1.23e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240  592 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
679-746 4.25e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 4.25e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 679 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 746
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-216 2.28e-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: 64.69  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    2 LQQEL--LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTK 79
Cdd:TIGR02168  218 LKAELreLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   80 SLMAKLSSMK-----------IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDR 148
Cdd:TIGR02168  295 NEISRLEQQKqilrerlanleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESR 373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240  149 DENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRykkmQDTVVLAQGKKGKDGEYEE 216
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER----LQQEIEELLKKLEEAELKE 437
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 523-578 5.29e-09

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 53.01  E-value: 5.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535240 523 QVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 578
Cdd:cd09487     1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
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 ...
 591-653 3.90e-08

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 50.93  E-value: 3.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240 591 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 653
Cdd:cd09565     1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
20-196 8.92e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 8.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  20 MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKkLKSTKSLMAKLSSMKIKVGQMQYEK 99
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 100 QRMEQKWEslkdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE 179
Cdd:COG4717   149 EELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                         170
                  ....*....|....*..
gi 2462535240 180 KDRKIEDLRQCLNRYKK 196
Cdd:COG4717   225 LEEELEQLENELEAAAL 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
10-196 1.14e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  10 TSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLS 86
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  87 SmKIKvgqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKGEGVEIVDRDENFKKKLKEKNIEvqKM 166
Cdd:PRK03918  321 E-EIN------GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTPE--KL 389

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462535240 167 KKAVESLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKK 419
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2-197 1.87e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 53.00  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKL---KST 78
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  79 KSLMAklssmkikvgqMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveiVDRDENFKKKLKE 158
Cdd:COG1579    89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL-----------AELEAELEEKKAE 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462535240 159 KNIEVQKMKKAVESLMAANEEKDRKI-EDLrqcLNRYKKM 197
Cdd:COG1579   147 LDEELAELEAELEELEAEREELAAKIpPEL---LALYERI 183
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 517-578 1.97e-07

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 48.99  E-value: 1.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 517 AKWTKEQVCNWL-MEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 578
Cdd:cd09564     2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-196 3.58e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  21 AEISNLKLKLTAVEK-DRLDYEDKFRDTEgLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEK 99
Cdd:PRK03918  176 RRIERLEKFIKRTENiEELIKEKEKELEE-VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 100 QRMEQKWESLKDELASLKEQLEEKESEVKRLQE-----KLVCKMKGEGVEIVDRDENFKK---KLKEKNIEVQKMKKAVE 171
Cdd:PRK03918  255 RKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKrlsRLEEEINGIEERIKELE 334

                         170       180
                  ....*....|....*....|....*
gi 2462535240 172 SLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:PRK03918  335 EKEERLEELKKKLKELEKRLEELEE 359
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 596-651 3.67e-07

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 48.08  E-value: 3.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535240 596 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 651
Cdd:cd09506    10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 3-188 4.64e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   3 QQELLS-RTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEIN--------DLRLKVSEMDSerLQYEK 73
Cdd:TIGR04523 428 IERLKEtIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkELKSKEKELKK--LNEEK 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  74 KL--KSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQL--EEKESEVKRLQEKLVcKMKGEGVEIVDRD 149
Cdd:TIGR04523 506 KEleEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIE-ELKQTQKSLKKKQ 584

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462535240 150 ENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLR 188
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-196 7.07e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 7.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   12 LETQKLDLMAEISNLKLKLTAVEKDRLDYEDKfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIK 91
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   92 VGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVE 171
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773

                          170       180
                   ....*....|....*....|....*
gi 2462535240  172 SLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:COG4913    774 RIDALRARLNRAEEELERAMRAFNR 798
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 596-648 8.46e-07

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.54  E-value: 8.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 596 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 648
Cdd:cd09533     2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 676-745 1.03e-06

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 46.91  E-value: 1.03e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  676 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 745
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
592-652 1.54e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 592 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:pfam07647   5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-187 3.33e-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: 51.22  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    3 QQELLSRTSLETQKL-DLMAEISNLKLKLTAV--EKDRLDYE--DKFRDTEGLIQEINDL--RLKVSEMDSERLQYEKKL 75
Cdd:TIGR02169  725 IEQLEQEEEKLKERLeELEEDLSSLEQEIENVksELKELEARieELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   76 KSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL------VCKMKGEGVEIVDRD 149
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeeleeeLEELEAALRDLESRL 884

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462535240  150 ENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 187
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 519-580 3.54e-06

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 45.39  E-value: 3.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 519 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 580
Cdd:cd09505     5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 2-206 6.00e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 50.17  E-value: 6.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEindLRLKVSEMDSERLQYEKK------- 74
Cdd:pfam01576  365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE---LQARLSESERQRAELAEKlsklqse 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   75 LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWESLKDELASLKEQLEEkESEVKRLQEKLVC 136
Cdd:pfam01576  442 LESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQLS 520

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240  137 KMKGEGVEivdrdenFKKKLKEKNIEVQ-------KMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQG 206
Cdd:pfam01576  521 TLQAQLSD-------MKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
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 ...
 516-580 2.19e-05

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 43.32  E-value: 2.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240 516 FAKWTKEQVCNWL-MEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 580
Cdd:cd09562     1 FALWNGPTVVAWLeLWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
PTZ00121 PTZ00121
MAEBL; Provisional
 48-210 2.42e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   48 EGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLK---DELASLKEQLEEKE 124
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKA 1670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  125 SEVKRLQEKL--VCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVV 202
Cdd:PTZ00121  1671 EEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750


                   ....*...
gi 2462535240  203 LAQGKKGK 210
Cdd:PTZ00121  1751 KDEEEKKK 1758
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 593-651 3.78e-05

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 42.31  E-value: 3.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 593 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 651
Cdd:cd09530     1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
519-580 5.83e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 5.83e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240 519 WTKEQVCNWLMEQGLGSYLNS-GKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 580
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNfRDQGITGAELLLRLTLEDL-KRLGITSVGHRRKILKKIQEL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 515-580 6.64e-05

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


Pssm-ID: 188906  Cd Length: 65  Bit Score: 41.63  E-value: 6.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240 515 PFAKWTKEQVCNWLMEQGLGSYLNS-GKHWIaSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 580
Cdd:cd09507     1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 65-208 7.86e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  65 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL-----V 135
Cdd:COG3883    15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 136 CKMKGEGV-------------EIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVV 202
Cdd:COG3883    95 LYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174


                  ....*.
gi 2462535240 203 LAQGKK 208
Cdd:COG3883   175 AQQAEQ 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-197 1.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEK--DRLDYEDkFRDTEGLIQEIND-----LRLKVSEMDSERLQYE-K 73
Cdd:PRK03918  544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKelEELGFES-VEELEERLKELEPfyneyLELKDAEKELEREEKElK 622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  74 KLKST---------------KSLMAKLSSMKIKVGQMQYEkqRMEQKWESLKDELASLKEQLEEKES---EVKRLQEKLv 135
Cdd:PRK03918  623 KLEEEldkafeelaetekrlEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKrreEIKKTLEKL- 699

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 136 ckmkgegveivdrdENFKKKLKEKNIEVQKMKKAVEslmaaneekdrKIEDLRQCLNRYKKM 197
Cdd:PRK03918  700 --------------KEELEEREKAKKELEKLEKALE-----------RVEELREKVKKYKAL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-193 1.53e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSL 81
Cdd:COG4942    43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  82 MAKLSS-----MKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegVEIVDRDENFKKKL 156
Cdd:COG4942   123 ALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL--------AELEEERAALEALK 194

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462535240 157 KEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 193
Cdd:COG4942   195 AERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 519-580 1.67e-04

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


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 40.75  E-value: 1.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 519 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 580
Cdd:cd09501     4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 22-189 1.75e-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: 45.48  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  22 EISNLKLKLTAVEKDRLDYedkFRDTEGLIQEINDLRLKVSEMDSE----RLQYEKKLKSTKSLMAKLSSMKIKVGQMQY 97
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHY---LKEVEDLKTELEKEKLKNIELTAHcdklLLENKELTQEASDMTLELKKHQEDIINCKK 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  98 EKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKM-KGEGVEIVDRDENFKKKLKEKNIEVQ--KMKKAVESlm 174
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIEN-- 605

                         170
                  ....*....|....*
gi 2462535240 175 aaneeKDRKIEDLRQ 189
Cdd:pfam05483 606 -----KNKNIEELHQ 615
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
31-134 1.75e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  31 TAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 106
Cdd:COG2433   402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467

                          90       100
                  ....*....|....*....|....*...
gi 2462535240 107 ESLKDELASLKEQLEEKESEVKRLQEKL 134
Cdd:COG2433   468 SRLDREIERLERELEEERERIEELKRKL 495
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 11-188 2.60e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  11 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEmdserlQYEKKLKSTKSLMAKLssmkI 90
Cdd:PRK00409  524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEK------EAQQAIKEAKKEADEI----I 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  91 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK------------LVCKMKGEGVEIVDRDE------NF 152
Cdd:PRK00409  591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKqeelkvgdevkyLSLGQKGEVLSIPDDKEaivqagIM 670

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462535240 153 KKKLKEKNIEVQKMKKAVESLMAANE-EKDRKIE---DLR 188
Cdd:PRK00409  671 KMKVPLSDLEKIQKPKKKKKKKPKTVkPKPRTVSlelDLR 710
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 10-196 2.84e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  10 TSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSlmaklssmk 89
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ--------- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  90 iKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEG---VEIVD----RDENFKKKLKEKNIE 162
Cdd:TIGR04523 240 -EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDlnnqKEQDWNKELKSELKN 318

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462535240 163 VQKMKKAVESLMAANEEkdrKIEDLRQCLNRYKK 196
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNK---IISQLNEQISQLKK 349
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 596-653 3.06e-04

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


Pssm-ID: 188946  Cd Length: 64  Bit Score: 39.87  E-value: 3.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535240 596 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 653
Cdd:cd09547     6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 52-189 3.21e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  52 QEINDLRLKVSEmdsERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWESLKDELASLKEQLEEK-------- 123
Cdd:PRK00409  516 EKLNELIASLEE---LERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikea 582

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 124 ESEVKRLQEKLVCKMKGEGVEIVDRD-ENFKKKLKEKNIEVQKMKKAVESLMAANEEKDR-KIEDLRQ 189
Cdd:PRK00409  583 KKEADEIIKELRQLQKGGYASVKAHElIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvKYLSLGQ 650
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-196 3.25e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  22 EISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKL-----KSTKSLMAKLSSMK------I 90
Cdd:PRK03918  526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyneyL 605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  91 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEivdRDENFKKKLKEKNIEVQKMKKAV 170
Cdd:PRK03918  606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAEL 682

                         170       180
                  ....*....|....*....|....*.
gi 2462535240 171 ESLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:PRK03918  683 EELEKRREEIKKTLEKLKEELEEREK 708
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 522-573 4.76e-04

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


Pssm-ID: 188896  Cd Length: 66  Bit Score: 39.16  E-value: 4.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535240 522 EQVCNWLMEQGLGSYLNsgkHWIASG---QTLLQASQQDLeKELGIKHSLHRKKL 573
Cdd:cd09497     5 EAIFDWLREFGLEEYTP---NFIKAGydlPTISRMTPEDL-TAIGITKPGHRKKL 55
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 515-571 4.93e-04

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


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 39.17  E-value: 4.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535240 515 PFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGI-----KHSLHRK 571
Cdd:cd09512     3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 593-652 4.94e-04

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


Pssm-ID: 188951  Cd Length: 71  Bit Score: 39.22  E-value: 4.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 593 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:cd09552     6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 11-215 6.28e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   11 SLETQKLDLMAEISNLKLKLTAVE--KDRLDyeDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTK-SLMAKLSS 87
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKilKDKKD--AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERdQLLNEVKT 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   88 MKIKVGQM--QYE--KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEV 163
Cdd:pfam15921  665 SRNELNSLseDYEvlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMKVAMGMQKQITAKRGQI 743

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535240  164 QKMKKAV----ESLMAANEEKDRKIEDlrqclnRYKKMQDTVVLAQGKKGKDGEYE 215
Cdd:pfam15921  744 DALQSKIqfleEAMTNANKEKHFLKEE------KNKLSQELSTVATEKNKMAGELE 793
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-196 6.31e-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: 43.52  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   98 EKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL------VCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVE 171
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100
                   ....*....|....*....|....*
gi 2462535240  172 SLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEE 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
13-199 6.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  13 ETQKLDLMAEisnLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMdserLQYEKKLKSTKSLMAKLSSMKIKv 92
Cdd:PRK03918  447 EEHRKELLEE---YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL----IKLKELAEQLKELEEKLKKYNLE- 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  93 gqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckMKGEGVEIvdrdenfKKKLKEKNIEVQKMKKAVES 172
Cdd:PRK03918  519 -----ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-----LKKKLAEL-------EKKLDELEEELAELLKELEE 581

                         170       180
                  ....*....|....*....|....*...
gi 2462535240 173 L-MAANEEKDRKIEDLRQCLNRYKKMQD 199
Cdd:PRK03918  582 LgFESVEELEERLKELEPFYNEYLELKD 609
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 17-187 7.17e-04

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.82  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  17 LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLR--LKVSEMDSERLQ-----YEKKLKSTKSLMAKLSSMK 89
Cdd:pfam13851  22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTepLQKAQEEVEELRkqlenYEKDKQSLKNLKARLKVLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  90 IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKR--------LQEKLvcKMKGEGVEIvdRDENFKKKLKEKNI 161
Cdd:pfam13851  99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAANL 174

                         170       180
                  ....*....|....*....|....*.
gi 2462535240 162 EVQKMKKAVESLMAANEEKDRKIEDL 187
Cdd:pfam13851 175 DPDALQAVTEKLEDVLESKNQLIKDL 200
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 517-565 7.29e-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: 7.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 517 AKWTKEQVCNWL--MEQGLGSYLNSGKHWIASGQTLLQASQQDLEkELGIK 565
Cdd:cd09511     2 AKWSPKQVTDWLkgLDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
53-189 7.89e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  53 EINDLRLKVSEMDSERL-QYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQ 131
Cdd:COG4372    14 SLFGLRPKTGILIAALSeQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535240 132 EKLVC------KMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 189
Cdd:COG4372    94 AELAQaqeeleSLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 9-215 9.12e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    9 RTSLETQKLDLMAEISNLKLKLTAVE---------KDRLDYedKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTK 79
Cdd:pfam15921  488 KMTLESSERTVSDLTASLQEKERAIEatnaeitklRSRVDL--KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   80 SLMAKLSSMKIKVGQ-------MQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGVEIVDRDENF 152
Cdd:pfam15921  566 ILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR-VSDLELEKVKLVNAGSER 644

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535240  153 KKKLKEknievqkmkkaveslmaANEEKDRKIEDLRQCLNRYKKM-QDTVVLAQGKKGKDGEYE 215
Cdd:pfam15921  645 LRAVKD-----------------IKQERDQLLNEVKTSRNELNSLsEDYEVLKRNFRNKSEEME 691
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 593-651 9.48e-04

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


Pssm-ID: 188887  Cd Length: 61  Bit Score: 38.37  E-value: 9.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 593 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 651
Cdd:cd09488     2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 519-560 1.10e-03

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


Pssm-ID: 188913  Cd Length: 72  Bit Score: 38.23  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462535240 519 WTKEQVCNWLMEQGLGSYLNSGKHWiaSGQTLLQASQQDLEK 560
Cdd:cd09514     7 WSPKEVSDWLSEEGMQEYSEALRSF--DGQALLNLTEEDFKK 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-189 1.22e-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: 42.74  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   52 QEINDLRLKVSEMDSERLQYEKKLKSTK------------------SLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDEL 113
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRkeleeleeeleqlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  114 ASLKEQLEE------------KESEVKRLQ-EKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEK 180
Cdd:TIGR02168  757 TELEAEIEEleerleeaeeelAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836


                   ....*....
gi 2462535240  181 DRKIEDLRQ 189
Cdd:TIGR02168  837 ERRLEDLEE 845
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 26-189 1.24e-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: 42.70  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  26 LKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQK 105
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----------EIERLKET 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 106 WESLKDELASLKEQLEEKESEVKRLqEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 185
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513


                  ....
gi 2462535240 186 DLRQ 189
Cdd:TIGR04523 514 DLTK 517
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1-200 1.28e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240    1 MLQQELLSRTSLETQKLDLMAEISNLKLKLTaVEKDRLDYEDKFRDTEGLIQEINDLRlKVSEMDSERLQYekklksTKS 80
Cdd:TIGR00606  793 IMERFQMELKDVERKIAQQAAKLQGSDLDRT-VQQVNQEKQEKQHELDTVVSKIELNR-KLIQDQQEQIQH------LKS 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   81 LMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKn 160
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE-KDQQEKEELISSKETSNKKAQDK- 942

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462535240  161 ieVQKMKKAVESLMAANEEKDRKIEDLRQclnRYKKMQDT 200
Cdd:TIGR00606  943 --VNDIKEKVKNIHGYMKDIENKIQDGKD---DYLKQKET 977
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-189 1.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   2 LQQELlsrTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSL 81
Cdd:COG1196   237 LEAEL---EELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARLEER 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  82 MAKLSSMKIKVGQmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegVEIVDRDENFKKKLKEKNI 161
Cdd:COG1196   311 RRELEERLEELEE---ELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--------AEAEEALLEAEAELAEAEE 379

                         170       180
                  ....*....|....*....|....*...
gi 2462535240 162 EVQKMKKAVESLMAANEEKDRKIEDLRQ 189
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEE 407
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 517-580 1.43e-03

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


Pssm-ID: 188914  Cd Length: 70  Bit Score: 38.00  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535240 517 AKWTKEQVCNWLMEQGLGSYLNS--GKHWIaSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 580
Cdd:cd09515     2 HEWTCEDVAKWLKKEGFSKYVDLlcNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
15-216 1.60e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  15 QKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDL--RLKVSEMDSERlqyEKKLkstkslMAKLSSM--KI 90
Cdd:COG1340    79 ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLewRQQTEVLSPEE---EKEL------VEKIKELekEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  91 KVGQMQYEKQRmeqKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAV 170
Cdd:COG1340   150 EKAKKALEKNE---KLKELRAELKELRKEAEEIHKKIKELAEE-AQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462535240 171 ESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGKDGEYEE 216
Cdd:COG1340   226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 519-563 1.87e-03

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


Pssm-ID: 188925  Cd Length: 66  Bit Score: 37.72  E-value: 1.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462535240 519 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQ---QDLEKELG 563
Cdd:cd09526     4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
PRK12704 PRK12704
phosphodiesterase; Provisional
 79-189 1.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  79 KSLMAKLSSMKIKVGQM--QYEKQRMEQKWESL---KDELASLKEQLE----EKESEVKRLQEKLVckmkgegveivDRD 149
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRIleEAKKEAEAIKKEALleaKEEIHKLRNEFEkelrERRNELQKLEKRLL-----------QKE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462535240 150 ENFKKK---LKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 189
Cdd:PRK12704   96 ENLDRKlelLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 519-575 2.19e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.70  E-value: 2.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 519 WTKEQVCNWLMEQ-GLGSYLNSGKHWIASGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 575
Cdd:cd09504     5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 675-727 2.51e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 37.31  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462535240 675 EVQKWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 727
Cdd:cd09504     1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 40-209 2.62e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   40 YEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSsmkikvgqmqyekqrmeQKWESLKDELASLKEQ 119
Cdd:smart00787 135 YEWRMKLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPKLR-----------------DRKDALEEELRQLKQL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  120 LEEKES----EVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR-Y 194
Cdd:smart00787 195 EDELEDcdptELDRAKEKLK-KLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKeI 273

                          170
                   ....*....|....*
gi 2462535240  195 KKMQDTVVLAQGKKG 209
Cdd:smart00787 274 EKLKEQLKLLQSLTG 288
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
11-135 2.73e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  11 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQ-------------EINDLRLKVSEMDSERLQYEKKLKS 77
Cdd:COG3206   209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpellqspVIQQLRAQLAELEAELAELSARYTP 288

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535240  78 T----KSLMAKLSSMKikvGQMQYEKQR----MEQKWESLKDELASLKEQLEEKESEVKRLQEKLV 135
Cdd:COG3206   289 NhpdvIALRAQIAALR---AQLQQEAQRilasLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 593-652 2.91e-03

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


Pssm-ID: 188948  Cd Length: 70  Bit Score: 37.15  E-value: 2.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 593 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 652
Cdd:cd09549     7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 596-652 3.15e-03

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


Pssm-ID: 188904  Cd Length: 72  Bit Score: 36.91  E-value: 3.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535240 596 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 652
Cdd:cd09505    10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 22-196 3.17e-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: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  22 EISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDlRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQR 101
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQ 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 102 MEQKWESLKDELASLKEQLEEKESEVKRLQEklvckmkgegveivdrdenfkkKLKEKNIEVQKMKKAVESLMAANEEKD 181
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQR----------------------ELEEKQNEIEKLKKENQSYKQEIKNLE 390

                         170
                  ....*....|....*
gi 2462535240 182 RKIEDLRQCLNRYKK 196
Cdd:TIGR04523 391 SQINDLESKIQNQEK 405
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 110-374 3.37e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  110 KDELASLKEQLEEKESEVKRLQEKLVCKM-------------KGEGVEIVDRDE----NFKKKLKEKNIEVQKMKKAVES 172
Cdd:PTZ00108  1101 KEKVEKLNAELEKKEKELEKLKNTTPKDMwledldkfeealeEQEEVEEKEIAKeqrlKSKTKGKASKLRKPKLKKKEKK 1180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  173 LMAANEEKDRKIEDLRqclnRYKKMQDTVVLAQGKKGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPScdp 252
Cdd:PTZ00108  1181 KKKSSADKSKKASVVG----NSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKS--- 1253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  253 fntsvPEEFHTTILQVSIPSLLPATVSMETSEKSKLTPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNL 331
Cdd:PTZ00108  1254 -----SEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462535240  332 KKETSDGEKetiqKTSEDRAPAESRPFGTLPPRPPGQDTSMDD 374
Cdd:PTZ00108  1329 KKTARKKKS----KTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-201 3.38e-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: 41.21  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   11 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRD-TEG---LIQE---------------INDLRLKVSEMDSERLQY 71
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEeqlRVKEkigeleaeiaslersIAEKERELEDAEERLAKL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   72 EKKLKSTKSLMAKLSSmkiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVC------KMKGEGVEI 145
Cdd:TIGR02169  328 EAEIDKLLAEIEELER---EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleKLKREINEL 404

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535240  146 VDRDENFKKKLKEKNIEVQKMKKAVES-------LMAANEEKDRKIEDLRQCLNRYKKMQDTV 201
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAAIAGieakineLEEEKEDKALEIKKQEWKLEQLAADLSKY 467
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 34-202 3.85e-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: 40.96  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  34 EKDRLDYEdKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKvgqmqyekqrMEQKWESLKDEL 113
Cdd:pfam10174 458 QREREDRE-RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK----------KDSKLKSLEIAV 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 114 ASLKEQLEEKESEVKRLQEKLVCKMKGEgvEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE-------KDRKIED 186
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVRTNP--EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAE 604

                         170
                  ....*....|....*.
gi 2462535240 187 LRQCLNRYKKMQDTVV 202
Cdd:pfam10174 605 LESLTLRQMKEQNKKV 620
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 68-185 3.88e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.80  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  68 RLQYEKKLKSTKSLMAKlssmkiKVGQMQYEKQRMEQKWESLKDELASLK---EQLEEKESEVKRLQEKLVCKMKGEGVE 144
Cdd:pfam10168 545 REEYLKKHDLAREEIQK------RVKLLKLQKEQQLQELQSLEEERKSLSeraEKLAEKYEEIKDKQEKLMRRCKKVLQR 618

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462535240 145 IVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 185
Cdd:pfam10168 619 LNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMN 659
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 62-216 4.48e-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: 40.82  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   62 SEMDSERLQYEKKLKStkSLMAKLSSMKIKVGQMQYEKQRMEQK-------WESLKDELASLKEQLEEKESEVKRLQEKL 134
Cdd:TIGR02169  676 LQRLRERLEGLKRELS--SLQSELRRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  135 vckmkgegVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAA-NEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGKDGE 213
Cdd:TIGR02169  754 --------ENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825


                   ...
gi 2462535240  214 YEE 216
Cdd:TIGR02169  826 LEK 828
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-187 4.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   2 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEIN--------DLRLKVSEMDSERLQYEK 73
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlqaaqaELAQAQEELESLQEEAEE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  74 KLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFK 153
Cdd:COG4372   113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462535240 154 KKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 187
Cdd:COG4372   193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 21-196 4.95e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   21 AEISNLKLKLTAVEKDRLDYEDKFRDtegLIQEINDLRLKV---SEMDSERLQYEKKLKSTKS--------LMAKLSSMK 89
Cdd:pfam01576   12 EELQKVKERQQKAESELKELEKKHQQ---LCEEKNALQEQLqaeTELCAEAEEMRARLAARKQeleeilheLESRLEEEE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   90 IKVGQMQYEKQRMEQkweslkdELASLKEQLEEKESEVKRLQ-EKLVCKMKGEGVE---IVDRDENFK----KKL----- 156
Cdd:pfam01576   89 ERSQQLQNEKKKMQQ-------HIQDLEEQLDEEEAARQKLQlEKVTTEAKIKKLEediLLLEDQNSKlskeRKLleeri 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535240  157 ----------KEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:pfam01576  162 seftsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-201 5.64e-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: 39.52  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  59 LKVSEMDSERLQYEKKLKStkslmaklssmkikvgqMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckm 138
Cdd:COG1579    10 LDLQELDSELDRLEHRLKE-----------------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535240 139 kgegVEIVDRDENFKKKLK-----------EKNIEVQKMKKAV--ESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 201
Cdd:COG1579    69 ----EEVEARIKKYEEQLGnvrnnkeyealQKEIESLKRRISDleDEILELMERIEELEEELAELEAELAELEAEL 140
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
72-197 5.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  72 EKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLqEKLVCKMKGEGVEIVDRDEN 151
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGS 253

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462535240 152 fKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKM 197
Cdd:PRK03918  254 -KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL 298
fliH PRK06669
flagellar assembly protein H; Validated
 23-187 6.02e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 39.61  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  23 ISNLKLKLTAVEKdrldYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTkslmAKLSSMKIKVGQMQYEKQRM 102
Cdd:PRK06669   12 INKEKLKTHEIQK----YRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEE----AEEDAFEIVEAAEEEAKEEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 103 EQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGveivdRDENFKKKLKEKNIEVQK-MKKAVESLMAANEEKD 181
Cdd:PRK06669   84 LKKTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEG-----YEEGYEKGREEGLEEVRElIEQLNKIIEKLIKKRE 158


                  ....*.
gi 2462535240 182 RKIEDL 187
Cdd:PRK06669  159 EILESS 164
Filament pfam00038
Intermediate filament protein;
11-197 6.31e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.52  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  11 SLETQKLDLMAEISNLKLkltAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLkstkslmaklssmki 90
Cdd:pfam00038  65 TLTVERARLQLELDNLRL---AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKI--------------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  91 kvgqmqyekqrmeqkwESLKDELASLKEQLEEkesEVKRLQEKLvckmkGEGVEIVDRDENFKKKLKE--KNIEVQKMKK 168
Cdd:pfam00038 127 ----------------ESLKEELAFLKKNHEE---EVRELQAQV-----SDTQVNVEMDAARKLDLTSalAEIRAQYEEI 182

                         170       180
                  ....*....|....*....|....*....
gi 2462535240 169 AVESLMAANEEKDRKIEDLRQCLNRYKKM 197
Cdd:pfam00038 183 AAKNREEAEEWYQSKLEELQQAAARNGDA 211
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
114-196 6.35e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240 114 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDEnfkKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 193
Cdd:COG2433   376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452


                  ...
gi 2462535240 194 YKK 196
Cdd:COG2433   453 ARS 455
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 593-640 6.38e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.16  E-value: 6.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535240 593 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 640
Cdd:cd09504     3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 7-196 7.96e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240   7 LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLS 86
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  87 SMKIKVgqmQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlvckmkgegveIVDRDENFKKKLKEKNIEVQK- 165
Cdd:TIGR04523 631 SIIKNI---KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK-----------IDDIIELMKDWLKELSLHYKKy 696

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462535240 166 -MKKAVESLMAANEEKDRKIEDLRQCLNRYKK 196
Cdd:TIGR04523 697 iTRMIRIKDLPKLEEKYKEIEKELKKLDEFSK 728
Cortex-I_coil pfam09304
Cortexillin I, coiled coil; Members of this family are predominantly found in the ...
 98-188 8.82e-03

Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.


Pssm-ID: 312712 [Multi-domain]  Cd Length: 107  Bit Score: 36.91  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  98 EKQRMEQKWESLKDELASLKEQLE-EKESEVKRLQEK-----LVCKMKGEGVEIVDRDENFKKKLKE--KNIEVQKMKKA 169
Cdd:pfam09304   3 EKERLEASKNSLANKLAGLENSLEsEKTSREQLIKQKdelesLLASLEQENAEREKRLRELEAKLDEalKNLELEKLARM 82

                          90
                  ....*....|....*....
gi 2462535240 170 VESLMAANEEKDRKIEDLR 188
Cdd:pfam09304  83 ELESRLSKTEKDKAILELK 101
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 21-189 9.40e-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: 39.81  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  21 AEISNLKLKLTAVEKDRLDYEDKFRDTEGLI--------QEINDLRLKVSEMDSERLQ-YEKKLKSTKSLMAKLSSMKIK 91
Cdd:pfam10174 579 AEVERLLGILREVENEKNDKDKKIAELESLTlrqmkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQQLQLE 658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535240  92 VGQMQYEKQRmeQKWESLKDELASLKEQLEEKESEV--------KRLQEKLVCKMKGEGVEIVDRDENFKkkLKEknIEV 163
Cdd:pfam10174 659 ELMGALEKTR--QELDATKARLSSTQQSLAEKDGHLtnlraerrKQLEEILEMKQEALLAAISEKDANIA--LLE--LSS 732

                         170       180
                  ....*....|....*....|....*.
gi 2462535240 164 QKMKKAVESLMAANEEKDRKIEDLRQ 189
Cdd:pfam10174 733 SKKKKTQEEVMALKREKDRLVHQLKQ 758
 
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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