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Conserved domains on  [gi|1370463065|ref|XP_024305004|]
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liprin-beta-1 isoform X7 [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 ...
 814-885 6.34e-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: 158.77  E-value: 6.34e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  814 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 729-791 7.76e-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: 135.51  E-value: 7.76e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09566      1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 655-718 5.13e-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: 124.65  E-value: 5.13e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463065  655 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-331 1.80e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMK-----------IKVGQMQYE 251
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanleRQLEELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  252 KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdievQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAEL------------------EELEAELEELESRLEELEEQLETLRS 386
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 814-885 6.34e-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: 158.77  E-value: 6.34e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  814 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 729-791 7.76e-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: 135.51  E-value: 7.76e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09566      1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 655-718 5.13e-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: 124.65  E-value: 5.13e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463065  655 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 731-791 2.45e-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: 2.45e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 657-719 1.07e-14

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 1.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  657 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 719
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 655-719 4.99e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 61.93  E-value: 4.99e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065   655 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 731-791 1.51e-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: 1.51e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 5.33e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 5.33e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-331 1.80e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMK-----------IKVGQMQYE 251
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanleRQLEELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  252 KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdievQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAEL------------------EELEAELEELESRLEELEEQLETLRS 386
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-337 1.86e-09

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: 61.66  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFR-----------DTEG 202
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEA 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  203 LIQEINDLR----LKVSEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQRMEQ--KWESLKD-ELASLKEQLE 274
Cdd:pfam05483  336 QMEELNKAKaahsFVVTEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKSSELEEmtKFKNNKEvELEELKKILA 415

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  275 EKESEV--KRLQEKLVCKMKGEGVEIV----DRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:pfam05483  416 EDEKLLdeKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-335 1.55e-08

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: 57.85  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  195 DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWESLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  267 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-338 6.77e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 6.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  258 KWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 1370463065  338 K 338
Cdd:PRK03918   419 K 419
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-884 1.23e-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: 1.23e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   815 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
 
Name Accession Description Interval E-value
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 814-885 6.34e-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: 158.77  E-value: 6.34e-46
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  814 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 729-791 7.76e-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: 135.51  E-value: 7.76e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  729 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09566      1 KLDTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 655-718 5.13e-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: 124.65  E-value: 5.13e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463065  655 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09563      1 FAEWSTEQVCDWLAELGLGQYVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQA 64
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 822-883 3.10e-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: 122.26  E-value: 3.10e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  822 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 883
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 818-885 2.31e-31

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


Pssm-ID: 188969  Cd Length: 72  Bit Score: 117.16  E-value: 2.31e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09570      5 WTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 734-791 2.20e-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: 2.20e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  734 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09495      2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 731-791 2.45e-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: 2.45e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 818-885 6.63e-18

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


Pssm-ID: 188967  Cd Length: 72  Bit Score: 78.90  E-value: 6.63e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 885
Cdd:cd09568      5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 657-719 1.07e-14

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.61  E-value: 1.07e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  657 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 719
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 ...
 663-718 4.94e-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: 67.25  E-value: 4.94e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463065  663 VCNWLMEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 718
Cdd:cd09494      2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 734-788 6.83e-13

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


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 64.18  E-value: 6.83e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065  734 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 788
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 729-791 1.15e-12

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


Pssm-ID: 188966  Cd Length: 65  Bit Score: 63.58  E-value: 1.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065  729 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09567      1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 655-719 4.99e-12

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


Pssm-ID: 197735  Cd Length: 68  Bit Score: 61.93  E-value: 4.99e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065   655 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 731-791 1.51e-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: 1.51e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065   731 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
818-885 5.33e-11

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 59.21  E-value: 5.33e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  818 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 885
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-331 1.80e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMK-----------IKVGQMQYE 251
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanleRQLEELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  252 KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdievQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAEL------------------EELEAELEELESRLEELEEQLETLRS 386
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 54-337 1.86e-09

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: 61.66  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFR-----------DTEG 202
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEA 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  203 LIQEINDLR----LKVSEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQRMEQ--KWESLKD-ELASLKEQLE 274
Cdd:pfam05483  336 QMEELNKAKaahsFVVTEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKSSELEEmtKFKNNKEvELEELKKILA 415

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  275 EKESEV--KRLQEKLVCKMKGEGVEIV----DRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:pfam05483  416 EDEKLLdeKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-329 4.98e-09

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: 60.47  E-value: 4.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   90 MTNGHLPGNGDV-----YQERLARLENDKESLVLQVSVLTDQVEAQ----GEKIRDLEFCLEEHREKVNATEEMLQQELL 160
Cdd:TIGR02169  655 MTGGSRAPRGGIlfsrsEPAELQRLRERLEGLKRELSSLQSELRRIenrlDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  161 SRTSLEtqklDLMAEISNLKLKLTAV--EKDRLDYE--DKFRDTEGLIQEINDL--RLKVSEMDSERLQYEKKLKSTKSL 234
Cdd:TIGR02169  735 LKERLE----ELEEDLSSLEQEIENVksELKELEARieELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  235 MAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQ--------------LEEKESEVKRLQ---EKLVCKMKGEGVE 297
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQiksiekeienlngkKEELEEELEELEaalRDLESRLGDLKKE 890

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370463065  298 IVDRDIEVQKMKKAVESLMAANEEKDRKIEDL 329
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 662-717 7.32e-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: 52.63  E-value: 7.32e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  662 QVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 717
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-287 1.54e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQV-------SVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  176 ISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRM 255
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASL 885

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1370463065  256 EQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRREL 917
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-335 1.55e-08

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: 57.85  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  195 DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWESLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  267 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 730-792 4.76e-08

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


Pssm-ID: 188964  Cd Length: 66  Bit Score: 50.55  E-value: 4.76e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065  730 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 792
Cdd:cd09565      1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-338 6.77e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 6.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  258 KWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 1370463065  338 K 338
Cdd:PRK03918   419 K 419
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-338 1.66e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  180 KLKLTAVEKDRLDYEDKFRDTEGLIQEindLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNN----------EIERLEARL 409

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  260 ESLKDELASLKEQLEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKEL------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-338 1.83e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTD---QVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:PRK03918   192 EELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  180 KLKLTAVEKDRLD------YEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMqyekq 253
Cdd:PRK03918   272 KKEIEELEEKVKElkelkeKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----- 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  254 rmEQKWESLKDELASLKEQLEEKEsEVKRLQ---EKLVCKMKGEGVEIVDRDIE-VQKMKKAVE----SLMAANEEKDRK 325
Cdd:PRK03918   344 --KKKLKELEKRLEELEERHELYE-EAKAKKeelERLKKRLTGLTPEKLEKELEeLEKAKEEIEeeisKITARIGELKKE 420

                          250
                   ....*....|...
gi 1370463065  326 IEDLRQCLNRYKK 338
Cdd:PRK03918   421 IKELKKAIEELKK 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-287 2.01e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.38  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellSRTSLETQKLDL---------M 173
Cdd:COG4942     40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  174 AEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQ 249
Cdd:COG4942    117 GRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1370463065  250 YEKQRM----EQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942    195 AERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEA 236
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-355 2.36e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  142 EEHREKVnaTEEMLQQELLSRT--SLETQKLDLMAEISNLKLKLTAVEK-DRLDYEDKFRDTEgLIQEINDLRLKVSEMD 218
Cdd:PRK03918   144 DESREKV--VRQILGLDDYENAykNLGEVIKEIKRRIERLEKFIKRTENiEELIKEKEKELEE-VLREINEISSELPELR 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  219 SERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQE-----KLVCKMKG 293
Cdd:PRK03918   221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSE 300

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  294 EGVEIVDRDIEVQKMK-------KAVESLMAANEEKDRKIEDLRqclNRYKKMQDTVVLAQGKDGEYEE 355
Cdd:PRK03918   301 FYEEYLDELREIEKRLsrleeeiNGIEERIKELEEKEERLEELK---KKLKELEKRLEELEERHELYEE 366
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 656-717 2.75e-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: 48.60  E-value: 2.75e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  656 AKWTKEQVCNWL-MEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 717
Cdd:cd09564      2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-339 4.31e-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: 52.23  E-value: 4.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKL---KST 231
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  232 KSLMAklssmkikvgqMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKA 311
Cdd:COG1579     89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157

                          170       180
                   ....*....|....*....|....*....
gi 1370463065  312 VESLMAANEEKDRKI-EDLrqcLNRYKKM 339
Cdd:COG1579    158 LEELEAEREELAAKIpPEL---LALYERI 183
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 735-790 4.66e-07

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


Pssm-ID: 188905  Cd Length: 66  Bit Score: 47.70  E-value: 4.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09506     10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-351 6.14e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 6.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLV------------------------LQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ 157
Cdd:COG1196    234 LRELEAELEELEAELEeleaeleeleaelaeleaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  158 ELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRL-KVSEMDSERLQYEKKLKSTKSLMA 236
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeAEAELAEAEEELEELAEELLEALR 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  237 KLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLM 316
Cdd:COG1196    394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1370463065  317 AANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKDG 351
Cdd:COG1196    474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
104-318 6.34e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQqELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  184 TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQ-YEKQRMEQKWESL 262
Cdd:PRK03918   310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGLTPEKL 389

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  263 KDELASLKEQLEEKESEVKRLQEKLvCKMKGEGVEivdrdievqkMKKAVESLMAA 318
Cdd:PRK03918   390 EKELEELEKAKEEIEEEISKITARI-GELKKEIKE----------LKKAIEELKKA 434
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
152-338 1.12e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  152 EEMLQQEL--LSRTSLETQKLDLmAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEkKLK 229
Cdd:COG4717     48 LERLEKEAdeLFKPQGRKPELNL-KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  230 STKSLMAKLSSMKIKVGQMQYEKQRMEQKWEslkdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDrdiEVQKMK 309
Cdd:COG4717    126 QLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLA 198

                          170       180
                   ....*....|....*....|....*....
gi 1370463065  310 KAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:COG4717    199 EELEELQQRLAELEEELEEAQEELEELEE 227
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-329 1.17e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEkdrLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWESL 262
Cdd:TIGR04523  449 DSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE----------EKKELEEKVKDL 515

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  263 KDELASLKEQLEEKESEVKRLQEKLVCK----------MKGEGVEIVDRDI--EVQKMKKAVESLMAANEEKDRKIEDL 329
Cdd:TIGR04523  516 TKKISSLKEKIEKLESEKKEKESKISDLedelnkddfeLKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQK 594
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 735-787 1.22e-06

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


Pssm-ID: 188932  Cd Length: 58  Bit Score: 46.54  E-value: 1.22e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 787
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 815-884 1.23e-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: 1.23e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   815 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 884
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-331 1.33e-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: 52.76  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQEllsrtsleTQKLDLM 173
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--------NKKIKDL 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  174 AEISNLKLKltaveKDRLDYEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQ 253
Cdd:TIGR02169  285 GEEEQLRVK-----EKIGELEAEIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELER---EIEEERKRRD 353

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  254 RMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveiVDRDIEVQKMKKAVESLmaaNEEKDRKIEDLRQ 331
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-----------KDYREKLEKLKREINEL---KRELDRLQEELQR 417
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 103-329 1.44e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.33  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfcleehrEKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEKDRLDYEDKF-------RDTEG----LIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL------SSMKIKV 245
Cdd:TIGR04523  484 LEQKQKELKSKEKELkklneekKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkENLEKEI 563

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  246 GQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKGEGVEIVDRDIE-VQKMKKAVESLMAANEEKDR 324
Cdd:TIGR04523  564 DEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI--EEKEKKISSLEKELEkAKKENEKLSSIIKNIKSKKN 641


                   ....*
gi 1370463065  325 KIEDL 329
Cdd:TIGR04523  642 KLKQE 646
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
731-791 1.86e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 46.11  E-value: 1.86e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  731 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-330 2.16e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--VNATEEMLQQELLSRTSLETQKLDLMAEIS 177
Cdd:COG3206    159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  178 NLKLKLTAVEKDRLDYEDKFRDTEGlIQEINDLRLKVSEMDSERLQYEKKLKST----KSLMAKLSSMKikvGQMQYEKQ 253
Cdd:COG3206    237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALR---AQLQQEAQ 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  254 R----MEQKWESLKDELASLKEQLEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQK--MKKAVESLMAANEEKDRKIE 327
Cdd:COG3206    313 RilasLEAELEALQAREASLQAQLAQLEARLAELPELEA------ELRRLEREVEVARelYESLLQRLEEARLAEALTVG 386


                   ...
gi 1370463065  328 DLR 330
Cdd:COG3206    387 NVR 389
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-333 2.26e-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: 51.71  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  132 EKIRDLEFCLEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  208 ndLRLKVSEMDSERLQYEKK-------LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWESL 262
Cdd:pfam01576  417 --LQARLSESERQRAELAEKlsklqseLESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQL 494

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  263 KDELASLKEQLEEkESEVKRLQEKLVCKMKgegVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCL 333
Cdd:pfam01576  495 EDERNSLQEQLEE-EEEAKRNVERQLSTLQ---AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 104-331 2.34e-06

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: 51.65  E-value: 2.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  104 ERLARLENDKESLVLQVSvltdQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSletqkldlmaEISNLKLKL 183
Cdd:pfam05483  394 EEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  184 TAVEKDRLDYedkFRDTEGLIQEINDLRLKVSEMDSE----RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRM---- 255
Cdd:pfam05483  460 TAIKTSEEHY---LKEVEDLKTELEKEKLKNIELTAHcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEERMlkqi 536

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  256 ---EQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:pfam05483  537 enlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 658-719 4.19e-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: 4.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  658 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09505      5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-291 8.37e-06

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: 48.38  E-value: 8.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  207 INDLRLKVSEMDSERLQyekklkstksLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:COG1579     98 IESLKRRISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                   ....*
gi 1370463065  287 LVCKM 291
Cdd:COG1579    168 LAAKI 172
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 87-344 8.75e-06

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: 50.12  E-value: 8.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   87 QSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEA-QGEKIRDLEFCLEEHREKVnatEEMLQQELLSRTSL 165
Cdd:pfam15921  207 HDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRI---EQLISEHEVEITGL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFrdteglIQEINDLRLKVSEMDSE----RLQYEKKLKSTKSLMAKLSSm 241
Cdd:pfam15921  284 TEKASSARSQANSIQSQLEIIQEQARNQNSMY------MRQLSDLESTVSQLRSElreaKRMYEDKIEELEKQLVLANS- 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  242 kiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEV---KRLQEKLVCKMKGEGV-------EIVDRDIEVQKMKKA 311
Cdd:pfam15921  357 --ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDRDTGNSItidhlrrELDDRNMEVQRLEAL 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1370463065  312 VESL-----------MAANEEKD---RKIEDLRQCLNRYKKMQDTVV 344
Cdd:pfam15921  435 LKAMksecqgqmerqMAAIQGKNeslEKVSSLTAQLESTKEMLRKVV 481
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
104-318 1.32e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKvnateemlqqellsRTSLETqkldLMAEISNLKLKL 183
Cdd:PRK02224   206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER--------------REELET----LEAEIEDLRETI 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  184 TAVEKDRLDYEDKFRD----TEGLIQEINDLRlkvSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:PRK02224   268 AETEREREELAEEVRDlrerLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  260 ESLKDELASLKEQLEEKESEVKRLQEKLvckmKGEGVEIVDRDIEVQKMKKAVESLMAA 318
Cdd:PRK02224   345 ESLREDADDLEERAEELREEAAELESEL----EEAREAVEDRREEIEELEEEIEELRER 399
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 103-287 2.27e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEML---------QQELLS-------RTSLE 166
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaeieeRREELGeraralyRSGGS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  167 TQKLDLMAEISNLKlklTAVekDRLDYEDKFRDTEG-LIQEINDLRLKVSEmdsERLQYEKKLKSTKSLMAKLSSMKikv 245
Cdd:COG3883    102 VSYLDVLLGSESFS---DFL--DRLSALSKIADADAdLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAK--- 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1370463065  246 GQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG3883    171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 655-719 2.80e-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: 42.94  E-value: 2.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463065  655 FAKWTKEQVCNWL-MEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09562      1 FALWNGPTVVAWLeLWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-338 3.22e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  153 EMLQQELlsrTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDkfrdteglIQEINDLRLKVSEMDSERLQYEKKLKSTK 232
Cdd:COG4913    613 AALEAEL---AELEEELAEAEERLEALEAELDALQERREALQR--------LAEYSWDEIDVASAEREIAELEAELERLD 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  233 SLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGV-----------EIVDR 301
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralleerfaAALGD 761

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370463065  302 DIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:COG4913    762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
SAM_Samd14 cd09530
SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...
 732-790 4.39e-05

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


Pssm-ID: 188929  Cd Length: 67  Bit Score: 42.31  E-value: 4.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  732 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09530      1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 109-334 4.55e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEisnLKLKLTAVEK 188
Cdd:TIGR04523  300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  189 DRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKS-------------------------TKSLMAKLSSMKI 243
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKlqqekellekeierlketiiknnseIKDLTNQDSVKEL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  244 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRlQEKLVCKMKGEGVE----IVDRDIEVQKMKKAVESLMAAN 319
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS-KEKELKKLNEEKKEleekVKDLTKKISSLKEKIEKLESEK 533

                          250
                   ....*....|....*
gi 1370463065  320 EEKDRKIEDLRQCLN 334
Cdd:TIGR04523  534 KEKESKISDLEDELN 548
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
658-719 6.83e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 6.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  658 WTKEQVCNWLMEQGLGSYLNS-GKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
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 ...
 654-719 7.86e-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: 7.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463065  654 PFAKWTKEQVCNWLMEQGLGSYLNS-GKHWIaSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09507      1 PVTNWTTEEVGAWLESLQLGEYRDIfARNDI-RGSELLHLERRDL-KDLGITKVGHVKRILQAIKDL 65
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 68-331 8.38e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 8.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   68 EGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK 147
Cdd:pfam10174  453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  148 VNATEEML----QQELLSRTSLE-TQKLDLM---------------AEISNLKLKLTAVEKDRLDYEDKFRDTEGLI--- 204
Cdd:pfam10174  533 CSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrq 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  205 -----QEINDLRLKVSEMDSERLQ-YEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRmeQKWESLKDELASLKEQLEEKES 278
Cdd:pfam10174  613 mkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDG 690

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  279 EV--------KRLQEKLvcKMKGEGV--EIVDRDIEV-------QKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:pfam10174  691 HLtnlraerrKQLEEIL--EMKQEALlaAISEKDANIallelssSKKKKTQEEVMALKREKDRLVHQLKQ 758
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-287 8.93e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 8.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEE---MLQQELLS--------RTSLETQKLD 171
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAElekeiaelRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  172 L---------MAEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:COG4942    106 LaellralyrLGRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370463065  239 SSMKIKVGQMQYEKQRMEQKwesLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942    184 EEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
100-343 1.18e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.29  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  180 KLKLTAVEKDRLDYEDKFRDTEGLIQEI----------NDLRLKVSEMDSE---RLQYEKKLKSTKSLMAKLSSMKIKVG 246
Cdd:COG1340     98 RKELAELNKAGGSIDKLRKEIERLEWRQqtevlspeeeKELVEKIKELEKElekAKKALEKNEKLKELRAELKELRKEAE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  247 QMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckmkgegveivdrdiEVQKMKKAVESLMAANEEKDRKI 326
Cdd:COG1340    178 EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK------------------EIVEAQEKADELHEEIIELQKEL 239

                          250
                   ....*....|....*..
gi 1370463065  327 EDLRQCLNRYKKMQDTV 343
Cdd:COG1340    240 RELRKELKKLRKKQRAL 256
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 51-337 1.47e-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: 45.88  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   51 LVEDLRGLLEMMETDEKeglrcQIPDSTA-----ETLVEWLQSQMTNghLPGNGDVYQERLARLENDKESLvlqvSVLTD 125
Cdd:pfam15921  480 VVEELTAKKMTLESSER-----TVSDLTAslqekERAIEATNAEITK--LRSRVDLKLQELQHLKNEGDHL----RNVQT 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  126 QVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVE--KDRLDyeDKFRDTEGL 203
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilKDKKD--AKIRELEAR 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  204 IQEINDLRLKVSEMDSERLQYEKKLKSTK-SLMAKLSSMKIKVGQM--QYE--KQRMEQKWESLKDELASLKEQLEEKES 278
Cdd:pfam15921  627 VSDLELEKVKLVNAGSERLRAVKDIKQERdQLLNEVKTSRNELNSLseDYEvlKRNFRNKSEEMETTTNKLKMQLKSAQS 706

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  279 EVKRLQEKLVcKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:pfam15921  707 ELEQTRNTLK-SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-284 1.94e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQellsrtsletqkldlmaEISNL 179
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLER-----------------EIERL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  180 KLKLTAVEKDRLDYEDKFRdtegliqeindlRLKVSEMDSERlQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:COG4913    351 ERELEERERRRARLEALLA------------ALGLPLPASAE-EFAALRAEAAALLEALEE----------ELEALEEAL 407

                          170       180
                   ....*....|....*....|....*
gi 1370463065  260 ESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:COG4913    408 AEAEAALRDLRRELRELEAEIASLE 432
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 132-338 1.97e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  132 EKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDlR 211
Cdd:TIGR04523  211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-Q 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  212 LKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckm 291
Cdd:TIGR04523  290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR------ 363

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370463065  292 kgegvEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR04523  364 -----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 658-719 2.06e-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: 40.36  E-value: 2.06e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  658 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09501      4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
184-287 2.08e-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: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  184 TAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 259
Cdd:COG2433    402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467

                           90       100
                   ....*....|....*....|....*...
gi 1370463065  260 ESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG2433    468 SRLDREIERLERELEEERERIEELKRKL 495
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 102-344 2.62e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 45.12  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSL-------ETQKLDLMA 174
Cdd:pfam05557   25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALnkklnekESQLADARE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  175 EISNLKLKL----TAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKStkslmakLSSMKIKVGQMQY 250
Cdd:pfam05557  105 VISCLKNELselrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS-------LAEAEQRIKELEF 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  251 EKQRMEQKWESLKDELASLkEQLEEKESEVKRLQEklvckmkgegveivdrdiEVQKMKKAVESLMAANEEKdrkiEDLR 330
Cdd:pfam05557  178 EIQSQEQDSEIVKNSKSEL-ARIPELEKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLK 234

                          250
                   ....*....|....
gi 1370463065  331 QCLNRYKKMQDTVV 344
Cdd:pfam05557  235 RKLEREEKYREEAA 248
DUF16 pfam01519
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...
 105-156 3.02e-04

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


Pssm-ID: 396208 [Multi-domain]  Cd Length: 95  Bit Score: 40.97  E-value: 3.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQ 156
Cdd:pfam01519   26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 119-355 3.08e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKlkltaVEKDRLDYEdKFR 198
Cdd:pfam10174  395 KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLK-----EQREREDRE-RLE 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  199 DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL-SSMKIKVGQMQYEKQRMEQKweslKDELASLKEQLEEKE 277
Cdd:pfam10174  469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLaSSGLKKDSKLKSLEIAVEQK----KEECSKLENQLKKAH 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  278 S--EVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEE-------KDRKIEDLRQCLNRYKKMQDTVVlAQG 348
Cdd:pfam10174  545 NaeEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQNKKV-ANI 623


                   ....*..
gi 1370463065  349 KDGEYEE 355
Cdd:pfam10174  624 KHGQQEM 630
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 735-792 3.56e-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: 3.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463065  735 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 792
Cdd:cd09547      6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 654-710 3.79e-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: 39.94  E-value: 3.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  654 PFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGI-----KHSLHRK 710
Cdd:cd09512      3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 102-513 4.02e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 44.65  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLVlqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELlsrtslETQKLDLMAEISNLKL 181
Cdd:PTZ00108   986 YLVRLDLYKKRKEYLL---GKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKEL------KKLGYVRFKDIIKKKS 1056

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  182 KLTAVEKDrldyEDKFRDTEGLIQEINDLRLKVSEMDserlqYekklkstkslmakLSSMKIkvgqmqyekqrmeqkWES 261
Cdd:PTZ00108  1057 EKITAEEE----EGAEEDDEADDEDDEEELGAAVSYD-----Y-------------LLSMPI---------------WSL 1099

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  262 LKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESlmaANEEKDRKIEDLRQCLNRYKKMQD 341
Cdd:PTZ00108  1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEVEEKEI---AKEQRLKSKTKGKASKLRKPKLKK 1176

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  342 TVVLAQGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPSCDPFN----------------------TSVPEE 399
Cdd:PTZ00108  1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDeeqktkpkkssvkrlkskknnsSKSSED 1256

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  400 FHTTILQVSIPSLLPATVSMETSEKSKLTPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGNLKKETSDGE 478
Cdd:PTZ00108  1257 NDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK 1336

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1370463065  479 KetiqKTSEDRAPAESRPFGTLPPRPPGQDTSMDD 513
Cdd:PTZ00108  1337 S----KTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 218-287 4.17e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 4.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463065  218 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG3883     15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-327 4.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  183 LTAVEKDRLDYEdkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLssmkikvgqMQYEKQRMEQKWESL 262
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---------AEALENKIEDDEEEA 970

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  263 KDELASLKEQL-----------EEKESEVKRLQEklvckMKGEgveivDRDIEvqkmkKAVESLMAANEEKDRKIE 327
Cdd:TIGR02168  971 RRRLKRLENKIkelgpvnlaaiEEYEELKERYDF-----LTAQ-----KEDLT-----EAKETLEEAIEEIDREAR 1031
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 661-712 5.52e-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: 5.52e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370463065  661 EQVCNWLMEQGLGSYLNsgkHWIASG---QTLLQASQQDLeKELGIKHSLHRKKL 712
Cdd:cd09497      5 EAIFDWLREFGLEEYTP---NFIKAGydlPTISRMTPEDL-TAIGITKPGHRKKL 55
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 732-791 6.33e-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: 6.33e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  732 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09552      6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 134-330 7.06e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  134 IRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKdrldyedKFRDTEGLIQEINDLRLK 213
Cdd:TIGR04523  147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQ 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  214 VSEMDSERLQYEKKLKSTKSlmaklssmkiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKG 293
Cdd:TIGR04523  220 ISELKKQNNQLKDNIEKKQQ----------EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI--KELE 287

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1370463065  294 EGVEIVDRDIEVQKMKKAVESLMAANEE---KDRKIEDLR 330
Cdd:TIGR04523  288 KQLNQLKSEISDLNNQKEQDWNKELKSElknQEKKLEEIQ 327
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
76-335 7.52e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 7.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   76 DSTAETLVEW-LQSQMTNGhlpgNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM 154
Cdd:PRK02224   324 EELRDRLEECrVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE------------------INDLRLKVSE 216
Cdd:PRK02224   400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEE 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  217 MDSERLQYEKKLKSTKSLMAKLSSMKikvgQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGV 296
Cdd:PRK02224   480 LEAELEDLEEEVEEVEERLERAEDLV----EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAE 554

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1370463065  297 EIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:PRK02224   555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 84-333 8.60e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   84 EWLQSQMtNGHLPGNGDVYQERLA---RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELL 160
Cdd:pfam07888   30 ELLQNRL-EECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  161 SRTSLETQKLDLMAEisnlklkltavekdRLDYEDKFRDTEGLIQEINDlRLKVSEMDSERLQyekklKSTKSLMAKLSS 240
Cdd:pfam07888  109 SSEELSEEKDALLAQ--------------RAAHEARIRELEEDIKTLTQ-RVLERETELERMK-----ERAKKAGAQRKE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  241 MKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANE 320
Cdd:pfam07888  169 EEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT-ITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247

                          250
                   ....*....|...
gi 1370463065  321 EKDRKIEDLRQCL 333
Cdd:pfam07888  248 ASERKVEGLGEEL 260
SAM_CNK1,2,3-suppressor cd09511
SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...
 656-704 1.04e-03

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


Pssm-ID: 188910  Cd Length: 69  Bit Score: 38.43  E-value: 1.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  656 AKWTKEQVCNWL--MEQGLGSYLNSGKHWIASGQTLLQASQQDLEkELGIK 704
Cdd:cd09511      2 AKWSPKQVTDWLkgLDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 732-790 1.29e-03

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


Pssm-ID: 188887  Cd Length: 61  Bit Score: 37.98  E-value: 1.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 790
Cdd:cd09488      2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 103-338 1.31e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  168 QkldlMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMaklssmkikvgQ 247
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH-----------T 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  248 MQYEKQRMEQKWESLKDELASLKE---QLEEKESEVKRLQEKLV-----CKMKGEGVEIVDRDIE----VQKMKKAVESL 315
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQReqaTIDTRTSAFRDLQGQLAhakkqQELQQRYAELCAAAITctaqCEKLEKIHLQE 463

                          250       260
                   ....*....|....*....|....
gi 1370463065  316 MA-ANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR00618  464 SAqSLKEREQQLQTKEQIHLQETR 487
SAM_SGMS1 cd09514
SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...
 658-699 1.39e-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: 1.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370463065  658 WTKEQVCNWLMEQGLGSYLNSGKHWiaSGQTLLQASQQDLEK 699
Cdd:cd09514      7 WSPKEVSDWLSEEGMQEYSEALRSF--DGQALLNLTEEDFKK 46
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 164-326 1.41e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  164 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEmdserlQYEKKLKSTKSLMAKLssmkI 243
Cdd:PRK00409   524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEK------EAQQAIKEAKKEADEI----I 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  244 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK------------LVCKMKGEGVEIVD-RDIEVQ---- 306
Cdd:PRK00409   591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKqeelkvgdevkyLSLGQKGEVLSIPDdKEAIVQagim 670

                          170       180
                   ....*....|....*....|...
gi 1370463065  307 KMK---KAVESLMAANEEKDRKI 326
Cdd:PRK00409   671 KMKvplSDLEKIQKPKKKKKKKP 693
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 105-286 1.46e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 42.11  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  105 RLARLENDKESLVLQVSVLTDQveaqgEKIRDLEFCLEEHREKVNATEE--MLQQELLSRTSLETQK--LDLMAEISNLK 180
Cdd:pfam15905  130 QLLELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKevMAKQEGMEGKLQVTQKnlEHSKGKVAQLE 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  181 LKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVsEMDSERLQYEKKLKSTKS----------------LMAKLSSMKIK 244
Cdd:pfam15905  205 EKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNdeieslkqsleekeqeLSKQIKDLNEK 283

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1370463065  245 VGQMQYEKQRM----EQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:pfam15905  284 CKLLESEKEELlreyEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 656-719 1.49e-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: 1.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463065  656 AKWTKEQVCNWLMEQGLGSYLNS--GKHWIaSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 719
Cdd:cd09515      2 HEWTCEDVAKWLKKEGFSKYVDLlcNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-330 1.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  131 GEKIRDLEFCLEEHREK----VNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE 206
Cdd:COG4372      5 GEKVGKARLSLFGLRPKtgilIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  207 IN--------DLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKES 278
Cdd:COG4372     85 LNeqlqaaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370463065  279 EVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR 330
Cdd:COG4372    165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
127-331 1.68e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  127 VEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLKLTAVEkdrldyedkfrdtegliQE 206
Cdd:COG4372     26 IAALSEQLRKALFELDKLQEELEQLREELEQ-------AREELEQLEEELEQARSELEQLE-----------------EE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  207 INDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQE---ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1370463065  287 LvcKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:COG4372    159 L--ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 43-347 1.93e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   43 MGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAEtlvewLQSQMTNGHLPGngdVYQERLARLENDkeslVLQVSV 122
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPG---PLTRRMQRGEQT----YAQLET 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  123 LTDQVEAQGEKIRdlefcleEHREKVNATEEMLQQELLSRTSLETQkldlMAEISNLKLKLTAVEKDRLDYEDKFRDTEG 202
Cdd:TIGR00618  543 SEEDVYHQLTSER-------KQRASLKEQMQEIQQSFSILTQCDNR----SKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  203 LIQEINDLRLKVSEMDSERLQYEKKLKstKSLMAKLSSMKIKVGQMQYEKQRM---------EQKWES---LKDELASLK 270
Cdd:TIGR00618  612 CEQHALLRKLQPEQDLQDVRLHLQQCS--QELALKLTALHALQLTLTQERVREhalsirvlpKELLASrqlALQKMQSEK 689

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463065  271 EQLEEKESEVKRLQEKLVCKMKGEGveivDRDIEVQKMKKAVESLMAANEEKDrkiEDLRQCLNRYKKMQDTVVLAQ 347
Cdd:TIGR00618  690 EQLTYWKEMLAQCQTLLRELETHIE----EYDREFNEIENASSSLGSDLAARE---DALNQSLKELMHQARTVLKAR 759
SAM_Samd3 cd09526
SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...
 658-702 2.21e-03

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


Pssm-ID: 188925  Cd Length: 66  Bit Score: 37.72  E-value: 2.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1370463065  658 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQ---QDLEKELG 702
Cdd:cd09526      4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 170-329 2.31e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 40.27  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  170 LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLR--LKVSEMDSERLQ-----YEKKLKSTKSLMAKLSSMK 242
Cdd:pfam13851   22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTepLQKAQEEVEELRkqlenYEKDKQSLKNLKARLKVLE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  243 IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKR--------LQEKLvcKMKGEGVEIvdRDIEVQKMKKAV-- 312
Cdd:pfam13851   99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAAnl 174

                          170       180
                   ....*....|....*....|....*.
gi 1370463065  313 --ESLMAAN-------EEKDRKIEDL 329
Cdd:pfam13851  175 dpDALQAVTekledvlESKNQLIKDL 200
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 658-714 2.33e-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: 2.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  658 WTKEQVCNWLMEQ-GLGSYLNSGKHWIASGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 714
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 ...
 814-866 2.72e-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: 2.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370463065  814 EVQKWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 866
Cdd:cd09504      1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 215-344 2.75e-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: 41.98  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  215 SEMDSERLQYEKKLKStkSLMAKLSSMKIKVGQMQYEKQRMEQK-------WESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:TIGR02169  676 LQRLRERLEGLKRELS--SLQSELRRIENRLDELSQELSDASRKigeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  288 V---CKMKGEGVEIVDRDIEVQKMKKAVESLMAA-NEEKDRKIEDLRQCLNRYKKMQDTVV 344
Cdd:TIGR02169  754 EnvkSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARL 814
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 103-228 3.10e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM------------LQQEL----LSRTSLE 166
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370463065  167 TQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEG-LIQEINDLRLKVSEMDSERLQYEKKL 228
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAELEELEAEREELAAKI 172
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 114-315 3.25e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.53  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  114 ESLVLQVSVLTDQVEAQGEKIRDLEfcleehREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDY 193
Cdd:pfam08614    3 LELIDAYNRLLDRTALLEAENAKLQ------SEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  194 EDKFRDTEgliQEINDLRLKvSEMDSERLqyekklkstKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQL 273
Cdd:pfam08614   77 AQRLVDLN---EELQELEKK-LREDERRL---------AALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQL 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1370463065  274 EEKESEVKRLQEklvckmkgEGVEIVDRdiEVQKMKKAVESL 315
Cdd:pfam08614  144 NMAEEKLRKLEK--------ENRELVER--WMKRKGQEAEAM 175
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 735-791 3.59e-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: 3.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463065  735 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09505     10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
100-331 3.75e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  100 DVYQERLaRLENDKESLVLQVSVL-TDQVEAQ--GEKIRD--LEFCLEEHREKVNATEEMLQQELlsrTSLETQKLDLMA 174
Cdd:COG3206    121 ERLRKNL-TVEPVKGSNVIEISYTsPDPELAAavANALAEayLEQNLELRREEARKALEFLEEQL---PELRKELEEAEA 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  175 EISNLKLK--LTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLS------SMKIKVG 246
Cdd:COG3206    197 ALEEFRQKngLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQLA 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  247 QMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKI 326
Cdd:COG3206    274 ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353


                   ....*
gi 1370463065  327 EDLRQ 331
Cdd:COG3206    354 RRLER 358
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 732-791 4.37e-03

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


Pssm-ID: 188948  Cd Length: 70  Bit Score: 36.77  E-value: 4.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  732 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 791
Cdd:cd09549      7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-229 5.11e-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: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNAteemlqqellsrtsLETQKLDLMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370463065  182 KLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLK 229
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQRELAEAEAQAR 500
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 112-348 5.17e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 5.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  112 DKESLVLQVSVLTDQVEAQGEKIRDLEfcleehREKVNATEEMLQQellsrtsLETQKLDLMAEISNLKLKLTAVEKDrl 191
Cdd:COG5185    240 DPESELEDLAQTSDKLEKLVEQNTDLR------LEKLGENAESSKR-------LNENANNLIKQFENTKEKIAEYTKS-- 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  192 dyEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSM-----KIKVGQMQ----YEKQRMEQKWESL 262
Cdd:COG5185    305 --IDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLtenleAIKEEIENivgeVELSKSSEELDSF 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  263 KDELASLKEQLEEKESEVKRlQEKLVCKMKGEGVEIVDRDIEvqKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDT 342
Cdd:COG5185    383 KDTIESTKESLDEIPQNQRG-YAQEILATLEDTLKAADRQIE--ELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459


                   ....*.
gi 1370463065  343 VVLAQG 348
Cdd:COG5185    460 ESQSRL 465
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 111-340 5.51e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  111 NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAvekdr 190
Cdd:pfam15905   73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSE----- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  191 lDYEDKFRDTEG--LIQEINDLRLKVSEMDSERLQYEKKLKSTKSLM----AKLSSMKIKVgqMQYEKQRMEQKWESL-- 262
Cdd:pfam15905  148 -DGTQKKMSSLSmeLMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLehskGKVAQLEEKL--VSTEKEKIEEKSETEkl 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  263 -----------------KDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRK 325
Cdd:pfam15905  225 leyitelscvseqvekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQT 304

                          250       260
                   ....*....|....*....|...
gi 1370463065  326 I--------EDLRQCLNRYKKMQ 340
Cdd:pfam15905  305 LnaeleelkEKLTLEEQEHQKLQ 327
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 251-355 6.26e-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: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  251 EKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvcKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR 330
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ----ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100
                   ....*....|....*....|....*
gi 1370463065  331 QCLNRYKKMQDTVvlaQGKDGEYEE 355
Cdd:TIGR02169  751 QEIENVKSELKEL---EARIEELEE 772
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 106-284 6.35e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  106 LARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQkldLMAEISnlKLKLTA 185
Cdd:pfam05483  610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK---LLEEVE--KAKAIA 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  186 VEKDRLDYEDKFRdTEGLIQEIndlrlkVSEMDSERLQYEKKLKSTKSlmaKLSSMKIKVGQMQYEKQRMEQKWESLKDE 265
Cdd:pfam05483  685 DEAVKLQKEIDKR-CQHKIAEM------VALMEKHKHQYDKIIEERDS---ELGLYKNKEQEQSSAKAALEIELSNIKAE 754

                          170
                   ....*....|....*....
gi 1370463065  266 LASLKEQLEEKESEVKRLQ 284
Cdd:pfam05483  755 LLSLKKQLEIEKEEKEKLK 773
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 732-779 6.40e-03

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


Pssm-ID: 188903  Cd Length: 74  Bit Score: 36.54  E-value: 6.40e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463065  732 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 779
Cdd:cd09504      3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 234-334 6.74e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  234 LMAKLSSMKIKVGQ----MQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMK 309
Cdd:PRK00409   521 LIASLEELERELEQkaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGG 600

                           90       100
                   ....*....|....*....|....*
gi 1370463065  310 KAveslmaanEEKDRKIEDLRQCLN 334
Cdd:PRK00409   601 YA--------SVKAHELIEARKRLN 617
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
206-331 6.89e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  206 EINDLRLKVSEMDSERL-QYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:COG4372     14 SLFGLRPKTGILIAALSeQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1370463065  285 EKLVC---KMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:COG4372     94 AELAQaqeELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
Filament pfam00038
Intermediate filament protein;
125-287 6.91e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.90  E-value: 6.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  125 DQVEAQGEKIRDLEFCLEEHREK----VNATEEMLQQEL--LSRT--SLETQKLDLMAEISNLKLkltAVEKDRLDYEDK 196
Cdd:pfam00038   18 DKVRFLEQQNKLLETKISELRQKkgaePSRLYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  197 FRDTEGLIQEINDLRLKVSEMDSERLQYEKKLkstkslmaklssmkikvgqmqyekqrmeqkwESLKDELASLKEQLEEk 276
Cdd:pfam00038   95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKI-------------------------------ESLKEELAFLKKNHEE- 142

                          170
                   ....*....|.
gi 1370463065  277 esEVKRLQEKL 287
Cdd:pfam00038  143 --EVRELQAQV 151
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 146-338 7.04e-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: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  146 EKVNATEEMLQ--QELLSRTSLETQKLD-----LMAEISNLKLKLTA-------VEKDRLDYEDKFRDTEGLIQEInDLR 211
Cdd:pfam01576    5 EEMQAKEEELQkvKERQQKAESELKELEkkhqqLCEEKNALQEQLQAetelcaeAEEMRARLAARKQELEEILHEL-ESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  212 LKVSEMDSERLQYEKKLKST--KSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQlEEKESEVKRLQEKLVC 289
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERIS 162

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370463065  290 KMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:pfam01576  163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 205-325 7.09e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  205 QEINDLRLKVSEmdsERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWESLKDELASLKEQLEEK-------- 276
Cdd:PRK00409   516 EKLNELIASLEE---LERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikea 582

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1370463065  277 ESEVKRLQEKLVCKMKGEGVEIVDRDIevQKMKKAVEslmAANEEKDRK 325
Cdd:PRK00409   583 KKEADEIIKELRQLQKGGYASVKAHEL--IEARKRLN---KANEKKEKK 626
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
 103-330 8.01e-03

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


Pssm-ID: 462752 [Multi-domain]  Cd Length: 307  Bit Score: 39.57  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE-FCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:pfam09311   15 QEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEdKMNQLSEETSNQVSTLAKRNQKSETLLDELQQAFSQAKRNFQD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  182 KLTAVEKDRLDYEDKF----RDTEGLIqeiNDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmQYEKQRMEQ 257
Cdd:pfam09311   95 QLAVLMDSREQVSDELvrlqKDNESLQ---GKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEV---RTAADHMEE 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  258 KwesLKDELASLKEQLEEKESEVKRLQEKL---VCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR 330
Cdd:pfam09311  169 K---LKAEILFLKEQIQAEQCLKENLEETLqaeIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDLQ 241
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 80-284 8.14e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.36  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065   80 ETLVEWLQSQMTNGHLPGNGDVYQErLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQel 159
Cdd:pfam09787   24 EKLIASLKEGSGVEGLDSSTALTLE-LEELRQERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQE-- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  160 lSRTSLETQ---KLDLMAEISNLKLKLTAVEKD----RLDYEDKFRDTEgliQEINDLRLKV---SEMDSERLQYEKKLK 229
Cdd:pfam09787   98 -LEEQLATErsaRREAEAELERLQEELRYLEEElrrsKATLQSRIKDRE---AEIEKLRNQLtskSQSSSSQSELENRLH 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463065  230 S-TKSLMaklssmkikvgqmqyEKQRMeqkWESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:pfam09787  174 QlTETLI---------------QKQTM---LEALSTEKNSLVLQLERMEQQIKELQ 211
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-287 9.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  102 YQERLARLENDKESLvlqvsvltdqveaqGEKIRDLEFCLEEHREKVNATEEMLQQ----ELLSRTSLETQKLDL----- 172
Cdd:PRK03918   457 YTAELKRIEKELKEI--------------EEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLKKYNLeelek 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463065  173 -MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKL-----KSTKSLMAKLSSMK---- 242
Cdd:PRK03918   523 kAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyn 602

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1370463065  243 --IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:PRK03918   603 eyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
 
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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