NCBI Conserved Domain Search

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

713-773

2.84e-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: 79.62 E-value: 2.84e-18

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  713 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:pfam00536    4 SVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

639-701

1.17e-14

Pssm-ID: 425739 Cd Length: 64 Bit Score: 69.22 E-value: 1.17e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  639 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 701
Cdd:pfam00536    2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAIQRL 63

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

637-701

5.30e-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: 5.30e-12

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194   637 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 701
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

713-773

1.66e-11

Pssm-ID: 197735 Cd Length: 68 Bit Score: 60.39 E-value: 1.66e-11

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194   713 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

SAM_2

SAM domain (Sterile alpha motif);

800-867

5.44e-11

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 58.82 E-value: 5.44e-11

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  800 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 867
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

90-358

1.23e-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: 62.39 E-value: 1.23e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   90 MTNGHLPGNGDV-----YQERLARLENDKESLVLQVSVLTDQVEAQ----GEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:TIGR02169  655 MTGGSRAPRGGIlfsrsEPAELQRLRERLEGLKRELSSLQSELRRIenrlDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  161 SRTSLEtqklDLMAEISNLKLKLTAV--EKDRLDYE--DKFRDTEGLIQEINDL--RLKVSEMDSERLQYEKKLKSTKSL 234
Cdd:TIGR02169  735 LKERLE----ELEEDLSSLEQEIENVksELKELEARieELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  235 MAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQ---EKLVCKMKGEGVEIVDRDIEVQKMKKA 311
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKE 890

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535194  312 VESLMAANEEKDRKIEDLRQCLNRYKK-MQDTVVLAQGKKGKDGEYEE 358
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKrLSELKAKLEALEEELSEIED 938

SCP-1

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

54-337

2.78e-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: 61.28 E-value: 2.78e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFR-----------DT 200
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  201 EGLIQEINDLR----LKVSEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQRMEQ--KWESLKD-ELASLKEQ 272
Cdd:pfam05483  334 EAQMEELNKAKaahsFVVTEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKSSELEEmtKFKNNKEvELEELKKI 413

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  273 LEEKESEV--KRLQEKLVCKMKGEGVEIV----DRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:pfam05483  414 LAEDEKLLdeKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

115-335

4.98e-09

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 4.98e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  195 DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWESLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  267 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231

PRK03918

DNA double-strand break repair ATPase Rad50;

102-338

5.63e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.63e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  258 KWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 2462535194  338 K 338
Cdd:PRK03918   419 K 419

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

797-866

1.33e-06

Pssm-ID: 197735 Cd Length: 68 Bit Score: 46.52 E-value: 1.33e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   797 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 866
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 ...

796-867

6.45e-46

Pssm-ID: 188968 Cd Length: 72 Bit Score: 158.77 E-value: 6.45e-46

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  796 EVQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 867
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 ...

711-773

9.53e-38

Pssm-ID: 188965 Cd Length: 63 Bit Score: 135.13 E-value: 9.53e-38

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  711 KLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
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 ...

637-700

6.12e-34

Pssm-ID: 188962 Cd Length: 64 Bit Score: 124.26 E-value: 6.12e-34

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535194  637 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 700
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 ...

804-865

3.14e-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: 3.14e-33

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  804 RVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNL 865
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 ...

800-867

2.27e-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: 2.27e-31

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  800 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 867
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 ...

716-773

2.50e-20

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

Pssm-ID: 188894 Cd Length: 60 Bit Score: 85.28 E-value: 2.50e-20

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  716 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 773
Cdd:cd09495      2 WVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVhLKVTSQLHHLSLKCGIHVLH 60

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

713-773

2.84e-18

Pssm-ID: 425739 Cd Length: 64 Bit Score: 79.62 E-value: 2.84e-18

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  713 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
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 ...

800-867

7.24e-18

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

Pssm-ID: 188967 Cd Length: 72 Bit Score: 78.90 E-value: 7.24e-18

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  800 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATHFNLLI 867
Cdd:cd09568      5 WSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72

SAM_1

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...

639-701

1.17e-14

Pssm-ID: 425739 Cd Length: 64 Bit Score: 69.22 E-value: 1.17e-14

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  639 KWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKeLGIKHSLHRKKLQLALQAL 701
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 ...

645-700

5.25e-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: 5.25e-14

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  645 VCNWLMEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQA 700
Cdd:cd09494      2 VCAWLEDFGLMPmYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58

SAM_superfamily

cd09487

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...

716-770

7.25e-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: 63.80 E-value: 7.25e-13

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194  716 WVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQ 770
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 ...

711-773

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 2462535194  711 KLDFNWVTR-WLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 773
Cdd:cd09567      1 QLDHTWVAReWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKhLGVSKKFHQASLLRGIELLR 65

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

637-701

5.30e-12

Pssm-ID: 197735 Cd Length: 68 Bit Score: 61.93 E-value: 5.30e-12

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194   637 FAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 701
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

713-773

1.66e-11

Pssm-ID: 197735 Cd Length: 68 Bit Score: 60.39 E-value: 1.66e-11

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194   713 DFNWVTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTV-DDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:smart00454    5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

SAM_2

SAM domain (Sterile alpha motif);

800-867

5.44e-11

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 58.82 E-value: 5.44e-11

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  800 WTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLepRFNVETMAQLlniPPNKTLLRRHLATHFNLLI 867
Cdd:pfam07647    4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLL--RLTLEDLKRL---GITSVGHRRKILKKIQELK 66

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

90-358

1.23e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.23e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   90 MTNGHLPGNGDV-----YQERLARLENDKESLVLQVSVLTDQVEAQ----GEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:TIGR02169  655 MTGGSRAPRGGIlfsrsEPAELQRLRERLEGLKRELSSLQSELRRIenrlDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  161 SRTSLEtqklDLMAEISNLKLKLTAV--EKDRLDYE--DKFRDTEGLIQEINDL--RLKVSEMDSERLQYEKKLKSTKSL 234
Cdd:TIGR02169  735 LKERLE----ELEEDLSSLEQEIENVksELKELEARieELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  235 MAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQ---EKLVCKMKGEGVEIVDRDIEVQKMKKA 311
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKE 890

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535194  312 VESLMAANEEKDRKIEDLRQCLNRYKK-MQDTVVLAQGKKGKDGEYEE 358
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKrLSELKAKLEALEEELSEIED 938

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

103-331

1.32e-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: 62.38 E-value: 1.32e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEaQGEKIRDLEfclEEHREklnateemlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAE-KAERYKELK---AELRE-------------LELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  183 LTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMK-----------IKVGQMQYE 251
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanleRQLEELEAQ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  252 KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveivdrdievQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAEL------------------EELEAELEELESRLEELEEQLETLRS 386

SCP-1

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

54-337

2.78e-09

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 2.78e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   54 DLRGLLEMMETDEKEgLRCQIPDSTAETLVEWLQSQMTNGHLpgngdvyQERLARLENDKESlvlQVSVLTDQVEAQGEK 133
Cdd:pfam05483  187 DLNNNIEKMILAFEE-LRVQAENARLEMHFKLKEDHEKIQHL-------EEEYKKEINDKEK---QVSLLLIQITEKENK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  134 IRDLEFCLEEHREKLNATEE--MLQQELLSRtsLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFR-----------DT 200
Cdd:pfam05483  256 MKDLTFLLEESRDKANQLEEktKLQDENLKE--LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  201 EGLIQEINDLR----LKVSEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQRMEQ--KWESLKD-ELASLKEQ 272
Cdd:pfam05483  334 EAQMEELNKAKaahsFVVTEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKSSELEEmtKFKNNKEvELEELKKI 413

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  273 LEEKESEV--KRLQEKLVCKMKGEGVEIV----DRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:pfam05483  414 LAEDEKLLdeKKQFEKIAEELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

115-335

4.98e-09

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 4.98e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942      3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  195 DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWESLK---DEL 266
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRadlAEL 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  267 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231

SAM_superfamily

cd09487

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...

644-699

8.08e-09

Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 52.63 E-value: 8.08e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535194  644 QVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQ 699
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDL-KELGITSPGHRKKILRAIQ 55

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

103-287

8.90e-09

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 8.90e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSV-------LTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAE 175
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  176 ISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRM 255
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASL 885

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462535194  256 EQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRREL 917

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 ...

712-774

5.15e-08

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

Pssm-ID: 188964 Cd Length: 66 Bit Score: 50.55 E-value: 5.15e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194  712 LDFNWV-TRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLRI 774
Cdd:cd09565      1 MNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRThLKMVDSFHRTSLQYGILCLKR 65

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

100-338

5.24e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 5.24e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  180 KLKLTAVEKDRLDYEDKFRDTEGLIQEindLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNN----------EIERLEARL 409

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  260 ESLKDELASLKEQLEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKEL------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482

PRK03918

DNA double-strand break repair ATPase Rad50;

102-338

5.63e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.63e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLVLQVSVLTdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:PRK03918   181 LEKFIKRTENIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  182 KLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKV---SEMDSERLQYEKKLKSTKSLMAKLSSmKIKVGQMQYEK-QRMEQ 257
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAeeyIKLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKElEEKEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  258 KWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYK 337
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418


                   .
gi 2462535194  338 K 338
Cdd:PRK03918   419 K 419

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

103-287

6.17e-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: 55.93 E-value: 6.17e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQellSRTSLETQKLDL---------M 173
Cdd:COG4942     40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  174 AEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQ 249
Cdd:COG4942    117 GRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462535194  250 YEKQRM----EQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942    195 AERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEA 236

SAM_kazrin_repeat1

cd09564

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...

638-699

2.87e-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: 2.87e-07

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  638 AKWTKEQVCNWL-MEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQ 699
Cdd:cd09564      2 SRWKADMVLAWLeVVMHMPMYSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIE 64

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

155-339

3.23e-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: 52.62 E-value: 3.23e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKL---KST 231
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  232 KSLMAklssmkikvgqMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKA 311
Cdd:COG1579     89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157

                          170       180
                   ....*....|....*....|....*....
gi 2462535194  312 VESLMAANEEKDRKI-EDLrqcLNRYKKM 339
Cdd:COG1579    158 LEELEAEREELAAKIpPEL---LALYERI 183

Smc

COG1196

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

102-331

4.13e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.13e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLenDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:COG1196    218 LKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  182 KLTAVEKDRLDYEDKFRDTEG----LIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQR--- 254
Cdd:COG1196    296 ELARLEQDIARLEERRRELEErleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAela 375

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  255 -MEQKWESLKDELASLKEQLEEKESEVKRLQEklvckmkgegvEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:COG1196    376 eAEEELEELAEELLEALRAAAELAAQLEELEE-----------AEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

PRK03918

DNA double-strand break repair ATPase Rad50;

174-338

4.41e-07

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 4.41e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  174 AEISNLKLKLTAVEK-DRLDYEDKFRDTEgLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEK 252
Cdd:PRK03918   176 RRIERLEKFIKRTENiEELIKEKEKELEE-VLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  253 QRMEQKWESLKDELASLKEQLEEKESEVKRLQE-----KLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIE 327
Cdd:PRK03918   255 RKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334

                          170
                   ....*....|.
gi 2462535194  328 DLRQCLNRYKK 338
Cdd:PRK03918   335 EKEERLEELKK 345

SAM_Shank1,2,3

cd09506

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...

717-772

4.71e-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: 4.71e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535194  717 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 772
Cdd:cd09506     10 VGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

103-329

5.16e-07

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

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 5.16e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQV---EAQGEKIRDLEFCLEEHREKLNATEEMLQQELlsrTSLETQKLDLMAEISNL 179
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI---ERLKETIIKNNSEIKDL 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  180 KLKLTAVEkdrLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:TIGR04523  446 TNQDSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE----------EKKELEEKV 512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  260 ESLKDELASLKEQLEEKESEVKRLQEKLVCK----------MKGEGVEIVDRDI--EVQKMKKAVESLMAANEEKDRKIE 327
Cdd:TIGR04523  513 KDLTKKISSLKEKIEKLESEKKEKESKISDLedelnkddfeLKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELID 592


                   ..
gi 2462535194  328 DL 329
Cdd:TIGR04523  593 QK 594

SCP-1

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

104-331

6.28e-07

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 6.28e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  104 ERLARLENDKESLVLQVSvltdQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSletqkldlmaEISNLKLKL 183
Cdd:pfam05483  394 EEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQL 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  184 TAVEKDRLDYedkFRDTEGLIQEINDLRLKVSEM--DSERLQYEKK--LKSTKSLMAKLSSMKIKVGQMQYEKQRM---- 255
Cdd:pfam05483  460 TAIKTSEEHY---LKEVEDLKTELEKEKLKNIELtaHCDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMlkqi 536

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  256 ---EQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:pfam05483  537 enlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

103-329

6.33e-07

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 6.33e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE---FCLEEHREKLNATEEMLQQEL--LSRtSLETQKLDLMAEIS 177
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLkvLSR-SINKIKQNLEQKQK 489

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  178 NLKLK---LTAVEKDRLDYEDKFRDtegLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL------SSMKIKVGQM 248
Cdd:TIGR04523  490 ELKSKekeLKKLNEEKKELEEKVKD---LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkkENLEKEIDEK 566

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  249 QYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKGEGVEIVDRDIE-VQKMKKAVESLMAANEEKDRKIE 327
Cdd:TIGR04523  567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI--EEKEKKISSLEKELEkAKKENEKLSSIIKNIKSKKNKLK 644


                   ..
gi 2462535194  328 DL 329
Cdd:TIGR04523  645 QE 646

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

102-331

7.82e-07

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.82e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQEllsrtsleTQKLDLM 173
Cdd:TIGR02169  213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--------NKKIKDL 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  174 AEISNLKLKltaveKDRLDYEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQ 253
Cdd:TIGR02169  285 GEEEQLRVK-----EKIGELEAEIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELER---EIEEERKRRD 353

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  254 RMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveiVDRDIEVQKMKKAVESLmaaNEEKDRKIEDLRQ 331
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-----------KDYREKLEKLKREINEL---KRELDRLQEELQR 417

YhaN

COG4717

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

152-338

9.02e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 9.02e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  152 EEMLQQEL--LSRTSLETQKLDLmAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEkKLK 229
Cdd:COG4717     48 LERLEKEAdeLFKPQGRKPELNL-KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  230 STKSLMAKLSSMKIKVGQMQYEKQRMEQKWEslkdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDrdiEVQKMK 309
Cdd:COG4717    126 QLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLA 198

                          170       180
                   ....*....|....*....|....*....
gi 2462535194  310 KAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:COG4717    199 EELEELQQRLAELEEELEEAQEELEELEE 227

GumC

COG3206

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

100-330

1.12e-06

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 1.12e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--LNATEEMLQQELLSRTSLETQKLDLMAEIS 177
Cdd:COG3206    159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  178 NLKLKLTAVEKDRLDYEDKFRDTEGlIQEINDLRLKVSEMDSERLQYEKKLKST----KSLMAKLSSMKikvGQMQYEKQ 253
Cdd:COG3206    237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALR---AQLQQEAQ 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  254 R----MEQKWESLKDELASLKEQLEEKESEVKRLQEKLVckmkgeGVEIVDRDIEVQK--MKKAVESLMAANEEKDRKIE 327
Cdd:COG3206    313 RilasLEAELEALQAREASLQAQLAQLEARLAELPELEA------ELRRLEREVEVARelYESLLQRLEEARLAEALTVG 386


                   ...
gi 2462535194  328 DLR 330
Cdd:COG3206    387 NVR 389

SAM_Ste50-like_fungal

cd09533

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...

717-769

1.26e-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: 1.26e-06

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  717 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAI 769
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAV 54

SAM

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...

797-866

1.33e-06

Pssm-ID: 197735 Cd Length: 68 Bit Score: 46.52 E-value: 1.33e-06

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   797 VQKWTNHRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEprfnvETMAQLLNIPPNKTLLRRHLATHFNLL 866
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLL-----TSEEDLKELGITKLGHRKKILKAIQKL 65

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

132-333

1.40e-06

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

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 1.40e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  132 EKIRDLEFCLEEHREKLNATEEMLQQEL----LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEi 207
Cdd:pfam01576  338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  208 ndLRLKVSEMDSERLQYEKK-------LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWESL 262
Cdd:pfam01576  417 --LQARLSESERQRAELAEKlsklqseLESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQL 494

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  263 KDELASLKEQLEEkESEVKRLQEKLVCKMKgegVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCL 333
Cdd:pfam01576  495 EDERNSLQEQLEE-EEEAKRNVERQLSTLQ---AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561

SAM_2

SAM domain (Sterile alpha motif);

713-773

1.81e-06

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 46.11 E-value: 1.81e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  713 DFNWVTRWLDDIGLPQYKTQFDEGRVDG-RMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66

SAM_WDSUB1

cd09505

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...

640-701

3.99e-06

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

Pssm-ID: 188904 Cd Length: 72 Bit Score: 45.39 E-value: 3.99e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  640 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 701
Cdd:cd09505      5 WSEEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKDLKIESLGHRNKILRKIEEL 66

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

133-291

5.33e-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: 48.77 E-value: 5.33e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  133 KIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  207 INDLRLKVSEMDSERLQyekklkstksLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:COG1579     98 IESLKRRISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                   ....*
gi 2462535194  287 LVCKM 291
Cdd:COG1579    168 LAAKI 172

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

103-287

7.94e-06

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.94e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEML---------QQELLS-------RTSLE 166
Cdd:COG3883     22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaeieeRREELGeraralyRSGGS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  167 TQKLDLMAEISNLKlklTAVekDRLDYEDKFRDTEG-LIQEINDLRLKVSEmdsERLQYEKKLKSTKSLMAKLSSMKikv 245
Cdd:COG3883    102 VSYLDVLLGSESFS---DFL--DRLSALSKIADADAdLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAK--- 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462535194  246 GQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG3883    171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

Smc

COG1196

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

103-287

8.78e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 8.78e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDK--------------ESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQ 168
Cdd:COG1196    294 LAELARLEQDIarleerrreleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  169 KLDLMAEISNLKLKLTAVEKDRLDYEDKfrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQM 248
Cdd:COG1196    374 LAEAEEELEELAEELLEALRAAAELAAQ---LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEA 447

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462535194  249 QYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG1196    448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

87-344

8.93e-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: 49.73 E-value: 8.93e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   87 QSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEA-QGEKIRDLEFCLEEHREKLnatEEMLQQELLSRTSL 165
Cdd:pfam15921  207 HDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRI---EQLISEHEVEITGL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFrdteglIQEINDLRLKVSEMDSE----RLQYEKKLKSTKSLMAKLSSm 241
Cdd:pfam15921  284 TEKASSARSQANSIQSQLEIIQEQARNQNSMY------MRQLSDLESTVSQLRSElreaKRMYEDKIEELEKQLVLANS- 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  242 kiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEV---KRLQEKLVCKMKGEGV-------EIVDRDIEVQKMKKA 311
Cdd:pfam15921  357 --ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELsleKEQNKRLWDRDTGNSItidhlrrELDDRNMEVQRLEAL 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535194  312 VESL-----------MAANEEKD---RKIEDLRQCLNRYKKMQDTVV 344
Cdd:pfam15921  435 LKAMksecqgqmerqMAAIQGKNeslEKVSSLTAQLESTKEMLRKVV 481

PRK02224

DNA double-strand break repair Rad50 ATPase;

104-318

9.57e-06

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 9.57e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKlnateemlqqellsRTSLETqkldLMAEISNLKLKL 183
Cdd:PRK02224   206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER--------------REELET----LEAEIEDLRETI 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  184 TAVEKDRLDYEDKFRD----TEGLIQEINDLRlkvSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:PRK02224   268 AETEREREELAEEVRDlrerLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  260 ESLKDELASLKEQLEEKESEVKRLQEKLvckmKGEGVEIVDRDIEVQKMKKAVESLMAA 318
Cdd:PRK02224   345 ESLREDADDLEERAEELREEAAELESEL----EEAREAVEDRREEIEELEEEIEELRER 399

COG4913

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

145-338

1.13e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.13e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  145 REKLNAteemLQQELlsrTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDkfrdteglIQEINDLRLKVSEMDSERLQY 224
Cdd:COG4913    609 RAKLAA----LEAEL---AELEEELAEAEERLEALEAELDALQERREALQR--------LAEYSWDEIDVASAEREIAEL 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  225 EKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGV-------- 296
Cdd:COG4913    674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelrallee 753

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462535194  297 ---EIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:COG4913    754 rfaAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

109-358

2.14e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  109 LENDKESLVLqvSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEisnLKLKLTAVEK 188
Cdd:TIGR04523  300 LNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEK 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  189 DRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKS-------------------------TKSLMAKLSSMKI 243
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKlqqekellekeierlketiiknnseIKDLTNQDSVKEL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  244 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRlQEKLVCKMKGEGVE----IVDRDIEVQKMKKAVESLMAAN 319
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS-KEKELKKLNEEKKEleekVKDLTKKISSLKEKIEKLESEK 533

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462535194  320 EEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGKDGEYEE 358
Cdd:TIGR04523  534 KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE 572

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 ...

637-701

2.75e-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: 2.75e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  637 FAKWTKEQVCNWL-MEQGLGS-YLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 701
Cdd:cd09562      1 FALWNGPTVVAWLeLWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 67

SAM_Samd14

cd09530

SAM domain of Samd14 subfamily; SAM (sterile alpha motif) domain of SamD14 (or FAM15A) ...

714-772

4.31e-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: 4.31e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  714 FNW----VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 772
Cdd:cd09530      1 LSWdtedVAEWIEGLGFPQYRECFTTNFIDGRKLILVDASTLPRMGVTDFEHIKAIARKIREL 63

COG1340

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

100-358

4.81e-05

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 4.81e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  180 KLKLTAVEKDRLDYEDKFRDTEGLIQEI----------NDLRLKVSEMDSE---RLQYEKKLKSTKSLMAKLSSMKIKVG 246
Cdd:COG1340     98 RKELAELNKAGGSIDKLRKEIERLEWRQqtevlspeeeKELVEKIKELEKElekAKKALEKNEKLKELRAELKELRKEAE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  247 QMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckmkgegveivdrdiEVQKMKKAVESLMAANEEKDRKI 326
Cdd:COG1340    178 EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK------------------EIVEAQEKADELHEEIIELQKEL 239

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462535194  327 EDLRQCLNRYKKMQDTVVLAQGKKGKDGEYEE 358
Cdd:COG1340    240 RELRKELKKLRKKQRALKREKEKEELEEKAEE 271

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

103-287

5.86e-05

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.86e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEE---MLQQELLS--------RTSLETQKLD 171
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAElekeiaelRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  172 L---------MAEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:COG4942    106 LaellralyrLGRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535194  239 SSMKIKVGQMQYEKQRMEQKwesLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942    184 EEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229

SAM_2

SAM domain (Sterile alpha motif);

640-701

7.05e-05

SAM domain (Sterile alpha motif);

Pssm-ID: 429573 Cd Length: 66 Bit Score: 41.87 E-value: 7.05e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  640 WTKEQVCNWLMEQGLGSYLNS-GKHWIASGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 701
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 ...

636-701

8.27e-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: 8.27e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  636 PFAKWTKEQVCNWLMEQGLGSYLNS-GKHWIaSGQTLLQASQQDLeKELGIKHSLHRKKLQLALQAL 701
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

1.15e-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: 45.97 E-value: 1.15e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   68 EGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK 147
Cdd:pfam10174  453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  148 LNATEEML----QQELLSRTSLE-TQKLDLM---------------AEISNLKLKLTAVEKDRLDYEDKFRDTEGLI--- 204
Cdd:pfam10174  533 CSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrq 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  205 -----QEINDLRLKVSEMDSERLQ-YEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRmeQKWESLKDELASLKEQLEEKES 278
Cdd:pfam10174  613 mkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDG 690

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  279 EV--------KRLQEKLvcKMKGEGV--EIVDRDIEV-------QKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:pfam10174  691 HLtnlraerrKQLEEIL--EMKQEALlaAISEKDANIallelssSKKKKTQEEVMALKREKDRLVHQLKQ 758

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

103-352

1.16e-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: 45.89 E-value: 1.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMlqQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:pfam05557   51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA--REVISCLKNELSELRRQIQRAELELQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  183 LTAVEKDRLdyedkfrdtegliQEINDL-RLKVSEMDSERLQYEKKLKStkslmakLSSMKIKVGQMQYEKQRMEQKWES 261
Cdd:pfam05557  129 STNSELEEL-------------QERLDLlKAKASEAEQLRQNLEKQQSS-------LAEAEQRIKELEFEIQSQEQDSEI 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  262 LKDELASLkEQLEEKESEVKRLQEklvckmkgegveivdrdiEVQKMKKAVESLMAANEEKdrkiEDLRQCLNRYKKMQD 341
Cdd:pfam05557  189 VKNSKSEL-ARIPELEKELERLRE------------------HNKHLNENIENKLLLKEEV----EDLKRKLEREEKYRE 245

                          250
                   ....*....|.
gi 2462535194  342 TVVLAQGKKGK 352
Cdd:pfam05557  246 EAATLELEKEK 256

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

51-357

1.19e-04

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

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   51 LVEDLRGLLEMMETDEKeglrcQIPDSTA-----ETLVEWLQSQMTNghLPGNGDVYQERLARLENDKESLvlqvSVLTD 125
Cdd:pfam15921  480 VVEELTAKKMTLESSER-----TVSDLTAslqekERAIEATNAEITK--LRSRVDLKLQELQHLKNEGDHL----RNVQT 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  126 QVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVE--KDRLDyeDKFRDTEGL 203
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilKDKKD--AKIRELEAR 626

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  204 IQEINDLRLKVSEMDSERLQYEKKLKSTK-SLMAKLSSMKIKVGQM--QYE--KQRMEQKWESLKDELASLKEQLEEKES 278
Cdd:pfam15921  627 VSDLELEKVKLVNAGSERLRAVKDIKQERdQLLNEVKTSRNELNSLseDYEvlKRNFRNKSEEMETTTNKLKMQLKSAQS 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  279 EVKRLQEKLVcKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKM---------QDTVVLAQGK 349
Cdd:pfam15921  707 ELEQTRNTLK-SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFlkeeknklsQELSTVATEK 785


                   ....*...
gi 2462535194  350 KGKDGEYE 357
Cdd:pfam15921  786 NKMAGELE 793

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

103-327

1.39e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.39e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  183 LTAVEKDRLDYEdkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLssmkikVGQMQYEKQRMEQKWEsl 262
Cdd:TIGR02168  903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE------AEALENKIEDDEEEAR-- 971

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535194  263 kDELASLKEQL-----------EEKESEVKRLQEklvckMKGEgveivDRDIEvqkmkKAVESLMAANEEKDRKIE 327
Cdd:TIGR02168  972 -RRLKRLENKIkelgpvnlaaiEEYEELKERYDF-----LTAQ-----KEDLT-----EAKETLEEAIEEIDREAR 1031

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

141-338

1.60e-04

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  141 LEEHREKLNATEEMLQQELlsrTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDlRLKVSEMDSE 220
Cdd:TIGR04523  223 LKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  221 RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckmkgegvEIVD 300
Cdd:TIGR04523  299 DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR-----------ELEE 367

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462535194  301 RDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR04523  368 KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405

COG2433

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

184-287

1.82e-04

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.82e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  184 TAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 259
Cdd:COG2433    402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467

                           90       100
                   ....*....|....*....|....*...
gi 2462535194  260 ESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG2433    468 SRLDREIERLERELEEERERIEELKRKL 495

SAM_SARM1-like_repeat1

cd09501

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...

640-701

2.15e-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: 2.15e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  640 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLEKELGIKHSLHRKKLQLALQAL 701
Cdd:cd09501      4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRFLRELVEL 65

PLN02939

transferase, transferring glycosyl groups

63-343

2.43e-04

transferase, transferring glycosyl groups

Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 2.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   63 ETDEKEGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQ-ERLARLENDKESLVLQVSVLTDQVEAQGEKIRdLEFCL 141
Cdd:PLN02939   114 EQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQAlEDLEKILTEKEALQGKINILEMRLSETDARIK-LAAQE 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  142 EEHREKLNATEEMLQQELLSRTSLE-TQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSE 220
Cdd:PLN02939   193 KIHVEILEEQLEKLRNELLIRGATEgLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDAS 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  221 RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEK-QRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL----VCKMKGEG 295
Cdd:PLN02939   273 LRELESKFIVAQEDVSKLSPLQYDCWWEKVENlQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLkeanVSKFSSYK 352

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535194  296 VEIVDrdievQKMKKAVESLMAANEEKDRKIEDLRQCLnryKKMQDTV 343
Cdd:PLN02939   353 VELLQ-----QKLKLLEERLQASDHEIHSYIQLYQESI---KEFQDTL 392

COG4913

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

103-284

2.98e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.98e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAqgekirdlefcLEEHREKLNATEEMLQQELLsrtSLETQKLD-LMAEISNLKL 181
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELER-----------LEARLDALREELDELEAQIR---GNGGDRLEqLEREIERLER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  182 KLTAVEKDRLDYEDKFRdtegliqeindlRLKVSEMDSERlQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWES 261
Cdd:COG4913    353 ELEERERRRARLEALLA------------ALGLPLPASAE-EFAALRAEAAALLEALEE----------ELEALEEALAE 409

                          170       180
                   ....*....|....*....|...
gi 2462535194  262 LKDELASLKEQLEEKESEVKRLQ 284
Cdd:COG4913    410 AEAALRDLRRELRELEAEIASLE 432

DUF16

pfam01519

Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ...

105-156

3.08e-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: 3.08e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ 156
Cdd:pfam01519   26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

218-287

3.18e-04

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.18e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462535194  218 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG3883     15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88

SAM_EPH-A6

cd09547

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...

717-774

3.49e-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: 3.49e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462535194  717 VTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRI 774
Cdd:cd09547      6 VSDWLDSIKMGQYKNNFmAAGFTTLDMVSRMTIDDIRRIGVTLIGHQRRIVSSIQTLRL 64

PRK02224

DNA double-strand break repair Rad50 ATPase;

76-335

3.73e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.73e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   76 DSTAETLVEW-LQSQMTNGhlpgNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEM 154
Cdd:PRK02224   324 EELRDRLEECrVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE------------------INDLRLKVSE 216
Cdd:PRK02224   400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEE 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  217 MDSERLQYEKKLKSTKSLMAKLSSMKikvgQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGV 296
Cdd:PRK02224   480 LEAELEDLEEEVEEVEERLERAEDLV----EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAE 554

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2462535194  297 EIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 335
Cdd:PRK02224   555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593

SAM_Neurabin-like

cd09512

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...

636-692

3.91e-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: 39.56 E-value: 3.91e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462535194  636 PFAKWTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQQDLeKELGI-----KHSLHRK 692
Cdd:cd09512      3 PVSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGQQLLQLDSSKL-KALGItsssdRSLLKKK 63

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

134-330

4.11e-04

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 4.11e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  134 IRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKdrldyedKFRDTEGLIQEINDLRLK 213
Cdd:TIGR04523  147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL-------LLSNLKKKIQKNKSLESQ 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  214 VSEMDSERLQYEKKLKSTKSlmaklssmkiKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvcKMKG 293
Cdd:TIGR04523  220 ISELKKQNNQLKDNIEKKQQ----------EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI--KELE 287

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2462535194  294 EGVEIVDRDIEVQKMKKAVESLMAANEE---KDRKIEDLR 330
Cdd:TIGR04523  288 KQLNQLKSEISDLNNQKEQDWNKELKSElknQEKKLEEIQ 327

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

43-347

4.56e-04

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

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 4.56e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   43 MGSLRALHLVEDLRGLLEMMETDEKEGLRCQIPDSTAEtlvewLQSQMTNGHLPGngdVYQERLARLENDkeslVLQVSV 122
Cdd:TIGR00618  475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPG---PLTRRMQRGEQT----YAQLET 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  123 LTDQVEAQGEKIRdlefcleEHREKLNATEEMLQQELLSRTSLETQkldlMAEISNLKLKLTAVEKDRLDYEDKFRDTEG 202
Cdd:TIGR00618  543 SEEDVYHQLTSER-------KQRASLKEQMQEIQQSFSILTQCDNR----SKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  203 LIQEINDLRLKVSEMDSERLQYEKKLKstKSLMAKLSSMKIKVGQMQYEKQRM---------EQKWES---LKDELASLK 270
Cdd:TIGR00618  612 CEQHALLRKLQPEQDLQDVRLHLQQCS--QELALKLTALHALQLTLTQERVREhalsirvlpKELLASrqlALQKMQSEK 689

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  271 EQLEEKESEVKRLQEKLVCKMKGEGveivDRDIEVQKMKKAVESLMAANEEKDrkiEDLRQCLNRYKKMQDTVVLAQ 347
Cdd:TIGR00618  690 EQLTYWKEMLAQCQTLLRELETHIE----EYDREFNEIENASSSLGSDLAARE---DALNQSLKELMHQARTVLKAR 759

SAM_caskin1,2_repeat1

cd09497

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...

643-694

5.37e-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: 5.37e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194  643 EQVCNWLMEQGLGSYLNsgkHWIASG---QTLLQASQQDLeKELGIKHSLHRKKL 694
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 ...

714-773

6.04e-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: 6.04e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  714 FNWVTRWLDDIGLPQYKTQF-DEGRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:cd09552      6 FSTVDEWLDAIKMGQYKESFaNAGFTSFDVVSQMTMEDILRVGVTLAGHQKKILNSIQVMR 66

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

103-338

6.24e-04

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 6.24e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESL--VLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLN-------------ATEEMLQQELLSRTSLET 167
Cdd:TIGR00618  239 QQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaahikAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  168 QkldlMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMaklssmkikvgQ 247
Cdd:TIGR00618  319 K----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH-----------T 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  248 MQYEKQRMEQKWESLKDELASLKE---QLEEKESEVKRLQEKLV-----CKMKGEGVEIVDRDIE----VQKMKKAVESL 315
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQReqaTIDTRTSAFRDLQGQLAhakkqQELQQRYAELCAAAITctaqCEKLEKIHLQE 463

                          250       260
                   ....*....|....*....|....
gi 2462535194  316 MA-ANEEKDRKIEDLRQCLNRYKK 338
Cdd:TIGR00618  464 SAqSLKEREQQLQTKEQIHLQETR 487

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

105-286

6.33e-04

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: 43.26 E-value: 6.33e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  105 RLARLENDKESLVLQVSVLTDQveaqgEKIRDLEFCLEEHREKLNATEE--MLQQELLSRTSLETQK--LDLMAEISNLK 180
Cdd:pfam15905  130 QLLELTRVNELLKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKevMAKQEGMEGKLQVTQKnlEHSKGKVAQLE 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  181 LKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVsEMDSERLQYEKKLKSTKS----------------LMAKLSSMKIK 244
Cdd:pfam15905  205 EKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKEKNdeieslkqsleekeqeLSKQIKDLNEK 283

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462535194  245 VGQMQYEKQRM----EQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:pfam15905  284 CKLLESEKEELlreyEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

111-340

1.03e-03

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  111 NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAvekdr 190
Cdd:pfam15905   73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSE----- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  191 lDYEDKFRDTEG--LIQEINDLRLKVSEMDSERLQYEKKLKSTKSLM----AKLSSMKIKVgqMQYEKQRMEQKWESL-- 262
Cdd:pfam15905  148 -DGTQKKMSSLSmeLMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLehskGKVAQLEEKL--VSTEKEKIEEKSETEkl 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  263 -----------------KDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRK 325
Cdd:pfam15905  225 leyitelscvseqvekyKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQT 304

                          250       260
                   ....*....|....*....|...
gi 2462535194  326 I--------EDLRQCLNRYKKMQ 340
Cdd:pfam15905  305 LnaeleelkEKLTLEEQEHQKLQ 327

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

84-333

1.04e-03

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

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194   84 EWLQSQMtNGHLPGNGDVYQERLA---RLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELL 160
Cdd:pfam07888   30 ELLQNRL-EECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  161 SRTSLETQKLDLMAEisnlklkltavekdRLDYEDKFRDTEGLIQEINDlRLKVSEMDSERLQyekklKSTKSLMAKLSS 240
Cdd:pfam07888  109 SSEELSEEKDALLAQ--------------RAAHEARIRELEEDIKTLTQ-RVLERETELERMK-----ERAKKAGAQRKE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  241 MKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKlVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANE 320
Cdd:pfam07888  169 EEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT-ITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247

                          250
                   ....*....|...
gi 2462535194  321 EKDRKIEDLRQCL 333
Cdd:pfam07888  248 ASERKVEGLGEEL 260

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

125-330

1.06e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.06e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  125 DQVEAQGEKIRDLEFCLEEHREKLNAT-EEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGL 203
Cdd:COG4372      2 DRLGEKVGKARLSLFGLRPKTGILIAAlSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  204 IQEIN--------DLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEE 275
Cdd:COG4372     82 LEELNeqlqaaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462535194  276 KESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR 330
Cdd:COG4372    162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216

SAM_CNK1,2,3-suppressor

cd09511

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK ...

638-686

1.10e-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: 1.10e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  638 AKWTKEQVCNWL--MEQGLGSYLNSGKHWIASGQTLLQASQQDLEkELGIK 686
Cdd:cd09511      2 AKWSPKQVTDWLkgLDDCLQQYIYTFEREKVTGEQLLNLSPQDLE-NLGVT 51

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

103-344

1.24e-03

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.24e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQ------QELLSRTSLETQKLDLMAEI 176
Cdd:pfam10174  365 TKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkervKSLQTDSSNTDTALTTLEEA 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  177 SNLKLKLTAVEKDRLDYEDKFR--DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL-SSMKIKVGQMQYEKQ 253
Cdd:pfam10174  445 LSEKERIIERLKEQREREDRERleELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLaSSGLKKDSKLKSLEI 524

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  254 RMEQKweslKDELASLKEQLEEKES--EVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEE-------KDR 324
Cdd:pfam10174  525 AVEQK----KEECSKLENQLKKAHNaeEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDK 600

                          250       260
                   ....*....|....*....|
gi 2462535194  325 KIEDLRQCLNRYKKMQDTVV 344
Cdd:pfam10174  601 KIAELESLTLRQMKEQNKKV 620

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

164-326

1.29e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.29e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  164 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEmdserlQYEKKLKSTKSLMAKLssmkI 243
Cdd:PRK00409   524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEK------EAQQAIKEAKKEADEI----I 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  244 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK------------LVCKMKGEGVEIVD-RDIEVQ---- 306
Cdd:PRK00409   591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKqeelkvgdevkyLSLGQKGEVLSIPDdKEAIVQagim 670

                          170       180
                   ....*....|....*....|...
gi 2462535194  307 KMK---KAVESLMAANEEKDRKI 326
Cdd:PRK00409   671 KMKvplSDLEKIQKPKKKKKKKP 693

SAM_SGMS1

cd09514

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 ...

640-681

1.30e-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: 1.30e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2462535194  640 WTKEQVCNWLMEQGLGSYLNSGKHWiaSGQTLLQASQQDLEK 681
Cdd:cd09514      7 WSPKEVSDWLSEEGMQEYSEALRSF--DGQALLNLTEEDFKK 46

SAM_EPH-R

cd09488

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...

714-772

1.30e-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: 1.30e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  714 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVL 772
Cdd:cd09488      2 FRSVGEWLESIKMGRYKENFTAaGYTSLDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61

SAM_SGMS1-like

cd09515

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...

638-701

1.55e-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: 1.55e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  638 AKWTKEQVCNWLMEQGLGSYLNS--GKHWIaSGQTLLQASQQDL-EKELGIKHSLHRKKLQLALQAL 701
Cdd:cd09515      2 HEWTCEDVAKWLKKEGFSKYVDLlcNKHRI-DGKVLLSLTEEDLrSPPLEIKVLGDIKRLWLAIRKL 67

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

112-354

1.79e-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: 42.25 E-value: 1.79e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  112 DKESLVLQVSVLTDQVEAQGEKIRDLEfcleehREKLNATEEMLQQellsrtsLETQKLDLMAEISNLKLKLTAVEKDrl 191
Cdd:COG5185    240 DPESELEDLAQTSDKLEKLVEQNTDLR------LEKLGENAESSKR-------LNENANNLIKQFENTKEKIAEYTKS-- 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  192 dyEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSM-----KIKVGQMQ----YEKQRMEQKWESL 262
Cdd:COG5185    305 --IDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLtenleAIKEEIENivgeVELSKSSEELDSF 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  263 KDELASLKEQLEEKESEVKRlQEKLVCKMKGEGVEIVDRDIEvqKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDT 342
Cdd:COG5185    383 KDTIESTKESLDEIPQNQRG-YAQEILATLEDTLKAADRQIE--ELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459

                          250
                   ....*....|..
gi 2462535194  343 VVLAQGKKGKDG 354
Cdd:COG5185    460 ESQSRLEEAYDE 471

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

103-228

2.01e-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: 41.06 E-value: 2.01e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEM------------LQQEL----LSRTSLE 166
Cdd:COG1579     30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEIeslkRRISDLE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462535194  167 TQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEG-LIQEINDLRLKVSEMDSERLQYEKKL 228
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAeLDEELAELEAELEELEAEREELAAKI 172

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

170-329

2.14e-03

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

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.66 E-value: 2.14e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  170 LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLR--LKVSEMDSERLQ-----YEKKLKSTKSLMAKLSSMK 242
Cdd:pfam13851   22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTepLQKAQEEVEELRkqlenYEKDKQSLKNLKARLKVLE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  243 IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKR--------LQEKLvcKMKGEGVEIvdRDIEVQKMKKAV-- 312
Cdd:pfam13851   99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAAnl 174

                          170       180
                   ....*....|....*....|....*.
gi 2462535194  313 --ESLMAAN-------EEKDRKIEDL 329
Cdd:pfam13851  175 dpDALQAVTekledvlESKNQLIKDL 200

SAM_Samd3

cd09526

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a ...

640-684

2.15e-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: 2.15e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535194  640 WTKEQVCNWLMEQGLGSYLNSGKHWIASGQTLLQASQ---QDLEKELG 684
Cdd:cd09526      4 WSVEQVCNWLVEKNLGELVPRFQEEEVSGAALLALNDrmvQQLVKKIG 51

PTZ00121

MAEBL; Provisional

142-352

2.15e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.15e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  142 EEHR--EKLNATEEMLQQELLsRTSLETQKLDLMAEISNLKL--KLTAVEKDRLDYEDK---FRDTEGL-------IQEI 207
Cdd:PTZ00121  1519 EEAKkaDEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKnmaLRKAEEAkkaeearIEEV 1597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  208 NDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLK---DELASLKEQLEEKESEVKRLQ 284
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKAEEDKKKA 1677

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  285 EKL------------VCKMKGEGVEIVD--RDIEVQKMKKAvESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKK 350
Cdd:PTZ00121  1678 EEAkkaeedekkaaeALKKEAEEAKKAEelKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756


                   ..
gi 2462535194  351 GK 352
Cdd:PTZ00121  1757 KK 1758

GumC

COG3206

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

100-331

2.24e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.24e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  100 DVYQERLaRLENDKESLVLQVSVL-TDQVEAQ--GEKIRD--LEFCLEEHREKLNATEEMLQQELlsrTSLETQKLDLMA 174
Cdd:COG3206    121 ERLRKNL-TVEPVKGSNVIEISYTsPDPELAAavANALAEayLEQNLELRREEARKALEFLEEQL---PELRKELEEAEA 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  175 EISNLKLK--LTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLS------SMKIKVG 246
Cdd:COG3206    197 ALEEFRQKngLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQLA 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  247 QMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKI 326
Cdd:COG3206    274 ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353


                   ....*
gi 2462535194  327 EDLRQ 331
Cdd:COG3206    354 RRLER 358

SAM_STIM-1,2-like

cd09504

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...

640-696

2.26e-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: 2.26e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  640 WTKEQVCNWLMEQ-GLGSYLNSGKHWIASGQTLLQ-ASQQD--LEKELGIKHSLHRKKLQL 696
Cdd:cd09504      5 WTVEDTVEWLVNSvELPQYVEAFKENGVDGSALPRlAVNNPsfLTSVLGIKDPIHRQKLSL 65

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

146-338

2.35e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.35e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  146 EKLNATEEMLQ--QELLSRTSLETQKLD-----LMAEISNLKLKLTA-------VEKDRLDYEDKFRDTEGLIQEInDLR 211
Cdd:pfam01576    5 EEMQAKEEELQkvKERQQKAESELKELEkkhqqLCEEKNALQEQLQAetelcaeAEEMRARLAARKQELEEILHEL-ESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  212 LKVSEMDSERLQYEKKLKST--KSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQlEEKESEVKRLQEKLVC 289
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQ-NSKLSKERKLLEERIS 162

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535194  290 KMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 338
Cdd:pfam01576  163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211

PRK03918

DNA double-strand break repair ATPase Rad50;

102-287

2.75e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.75e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLvlqvsvltdqveaqGEKIRDLEFCLEEHREKLNATEEMLQQ----ELLSRTSLETQKLDL----- 172
Cdd:PRK03918   457 YTAELKRIEKELKEI--------------EEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLKKYNLeelek 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  173 -MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKL-----KSTKSLMAKLSSMK---- 242
Cdd:PRK03918   523 kAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyn 602

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462535194  243 --IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:PRK03918   603 eyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649

SAM_STIM-1,2-like

cd09504

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...

796-848

2.75e-03

Pssm-ID: 188903 Cd Length: 74 Bit Score: 37.31 E-value: 2.75e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462535194  796 EVQKWTNHRVMEWL-RSVDLAEYAPNLRGSGVHGGLMvlePRFNVETMAQLLNI 848
Cdd:cd09504      1 EVHNWTVEDTVEWLvNSVELPQYVEAFKENGVDGSAL---PRLAVNNPSFLTSV 51

Rab5-bind

pfam09311

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...

103-330

3.10e-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: 40.72 E-value: 3.10e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLE-FCLEEHREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:pfam09311   15 QEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEdKMNQLSEETSNQVSTLAKRNQKSETLLDELQQAFSQAKRNFQD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  182 KLTAVEKDRLDYEDKF----RDTEGLIqeiNDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmQYEKQRMEQ 257
Cdd:pfam09311   95 QLAVLMDSREQVSDELvrlqKDNESLQ---GKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEV---RTAADHMEE 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462535194  258 KwesLKDELASLKEQLEEKESEVKRLQEKL---VCKMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLR 330
Cdd:pfam09311  169 K---LKAEILFLKEQIQAEQCLKENLEETLqaeIENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQLEDLQ 241

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

103-287

3.13e-03

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

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 3.13e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVS-VLTDQVEAQGEKIRDLE------------FCLEEHREKLNATEEMLQ--QELLSRTSLET 167
Cdd:pfam12128  652 RLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEaqlkqldkkhqaWLEEQKEQKREARTEKQAywQVVEGALDAQL 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  168 QKLD--LMAEISNLKLKLTAVEKDRlDYEDKFRDTEG-----LIQEINDLRLKVSEMDSER---LQYEKKLKSTKSLmak 237
Cdd:pfam12128  732 ALLKaaIAARRSGAKAELKALETWY-KRDLASLGVDPdviakLKREIRTLERKIERIAVRRqevLRYFDWYQETWLQ--- 807

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535194  238 lssmkikvgqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:pfam12128  808 -------------RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKL 844

SCP-1

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

106-284

3.34e-03

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 3.34e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  106 LARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLETQkldLMAEISnlKLKLTA 185
Cdd:pfam05483  610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK---LLEEVE--KAKAIA 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  186 VEKDRLDYEDKFRdTEGLIQEIndlrlkVSEMDSERLQYEKKLKSTKSlmaKLSSMKIKVGQMQYEKQRMEQKWESLKDE 265
Cdd:pfam05483  685 DEAVKLQKEIDKR-CQHKIAEM------VALMEKHKHQYDKIIEERDS---ELGLYKNKEQEQSSAKAALEIELSNIKAE 754

                          170
                   ....*....|....*....
gi 2462535194  266 LASLKEQLEEKESEVKRLQ 284
Cdd:pfam05483  755 LLSLKKQLEIEKEEKEKLK 773

SAM_WDSUB1

cd09505

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...

717-773

3.49e-03

Pssm-ID: 188904 Cd Length: 72 Bit Score: 37.30 E-value: 3.49e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462535194  717 VTRWLDDIGLPQYKTQFDEGRVDGRMLHYMTVDDLLS-LKVVSVLHHLSIKRAIQVLR 773
Cdd:cd09505     10 VCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSKdLKIESLGHRNKILRKIEELK 67

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

234-352

3.61e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 3.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  234 LMAKLSSMKIKVGQ----MQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDIEVQKMK 309
Cdd:PRK00409   521 LIASLEELERELEQkaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGG 600

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462535194  310 KAveslmaanEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGK 352
Cdd:PRK00409   601 YA--------SVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

102-229

3.85e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.85e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNAteemlqqellsrtsLETQKLDLMAEISNLKL 181
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--------------LEEEKEDKALEIKKQEW 455

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462535194  182 KLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLK 229
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQRELAEAEAQAR 500

SAM_EPH-A10

cd09549

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...

714-773

4.09e-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: 4.09e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  714 FNWVTRWLDDIGLPQYKTQFDE-GRVDGRMLHYMTVDDLLSLKVVSVLHHLSIKRAIQVLR 773
Cdd:cd09549      7 FGSVGEWLEALDLCRYKDNFAAaGYGSLEAVARMTAQDVLSLGITSLEHQELLLAGIQALR 67

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

102-284

4.09e-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: 40.51 E-value: 4.09e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLV-------------------LQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLS- 161
Cdd:pfam09787   12 YKQKAARILQSKEKLIaslkegsgvegldsstaltLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESs 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  162 ---RTSLETQ-------KLDLMAEISNLKLKLTAVEKD----RLDYEDKFRDTEgliQEINDLRLKV---SEMDSERLQY 224
Cdd:pfam09787   92 reqLQELEEQlatersaRREAEAELERLQEELRYLEEElrrsKATLQSRIKDRE---AEIEKLRNQLtskSQSSSSQSEL 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  225 EKKLKS-TKSLMaklssmkikvgqmqyEKQRMeqkWESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:pfam09787  169 ENRLHQlTETLI---------------QKQTM---LEALSTEKNSLVLQLERMEQQIKELQ 211

YhaN

COG4717

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

103-288

4.21e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.21e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEAQG--EKIRDLEFCLEEHREKLnateEMLQQELLSRTSLETQKLDLMAEISNLK 180
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQ 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  181 lkltavekdrldyedkfrdtegliQEINDLRLKVSEMDSERLQyekklkstkslmaklssmkikvgQMQYEKQRMEQKWE 260
Cdd:COG4717    177 ------------------------EELEELLEQLSLATEEELQ-----------------------DLAEELEELQQRLA 209

                          170       180
                   ....*....|....*....|....*...
gi 2462535194  261 SLKDELASLKEQLEEKESEVKRLQEKLV 288
Cdd:COG4717    210 ELEEELEEAQEELEELEEELEQLENELE 237

YhaN

COG4717

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

116-340

4.39e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.39e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  116 LVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKLNATEEMLQQELLSRTSLE-----TQKLDLMAEISNLKLKLTAVEKDR 190
Cdd:COG4717    281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIEELQELLREAEELE 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  191 LDyedkfRDTEGLIQEINDLRLKVSEMDSERL-----QYEKKlkstKSLMAKLSSMKIKVGQMQYEKQRMEQKW--ESLK 263
Cdd:COG4717    361 EE-----LQLEELEQEIAALLAEAGVEDEEELraaleQAEEY----QELKEELEELEEQLEELLGELEELLEALdeEELE 431

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462535194  264 DELASLKEQLEEKESEVKRLQEklvckmkgegvEIVDRDIEVQKMKKAvESLMAANEEKDRKIEDLRQCLNRYKKMQ 340
Cdd:COG4717    432 EELEELEEELEELEEELEELRE-----------ELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALK 496

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

114-315

4.90e-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: 39.14 E-value: 4.90e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  114 ESLVLQVSVLTDQVEAQGEKIRDLEfcleehREKLNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDY 193
Cdd:pfam08614    3 LELIDAYNRLLDRTALLEAENAKLQ------SEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  194 EDKFRDTEgliQEINDLRLKvSEMDSERLqyekklkstKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQL 273
Cdd:pfam08614   77 AQRLVDLN---EELQELEKK-LREDERRL---------AALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQL 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462535194  274 EEKESEVKRLQEklvckmkgEGVEIVDRdiEVQKMKKAVESL 315
Cdd:pfam08614  144 NMAEEKLRKLEK--------ENRELVER--WMKRKGQEAEAM 175

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

206-331

5.03e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 5.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  206 EINDLRLKVSEMDSERL-QYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:COG4372     14 SLFGLRPKTGILIAALSeQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462535194  285 EKLVC---KMKGEGVEIVDRDIEVQKMKKAVESLMAANEEKDRKIEDLRQ 331
Cdd:COG4372     94 AELAQaqeELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

103-331

5.04e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  103 QERLARLENDKESLVLQVSVLTDQVEA--------QGEK------IRDLE---FCLEEHREKLNATEEMLQQELLSRTS- 164
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqklQLEKvtteakIKKLEediLLLEDQNSKLSKERKLLEERISEFTSn 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  165 ----------LETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGliqEINDLRLKVSEMDSE----RLQYEKKLKS 230
Cdd:pfam01576  168 laeeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG---ESTDLQEQIAELQAQiaelRAQLAKKEEE 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  231 TKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCkMKGEGVEIVD---------- 300
Cdd:pfam01576  245 LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA-LKTELEDTLDttaaqqelrs 323

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2462535194  301 -RDIEVQKMKKAVESLMAANEEkdrKIEDLRQ 331
Cdd:pfam01576  324 kREQEVTELKKALEEETRSHEA---QLQEMRQ 352

SAM_STIM-1,2-like

cd09504

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...

714-761

6.41e-03

Pssm-ID: 188903 Cd Length: 74 Bit Score: 36.54 E-value: 6.41e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462535194  714 FNW----VTRWL-DDIGLPQYKTQFDEGRVDGRML--------HYMTVDdllsLKVVSVLH 761
Cdd:cd09504      3 HNWtvedTVEWLvNSVELPQYVEAFKENGVDGSALprlavnnpSFLTSV----LGIKDPIH 59

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

205-325

6.55e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 6.55e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  205 QEINDLRLKVSEmdsERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWESLKDELASLKEQLEEK-------- 276
Cdd:PRK00409   516 EKLNELIASLEE---LERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikea 582

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462535194  277 ESEVKRLQEKLVCKMKGEGVEIVDRDIevQKMKKAVEslmAANEEKDRK 325
Cdd:PRK00409   583 KKEADEIIKELRQLQKGGYASVKAHEL--IEARKRLN---KANEKKEKK 626

PRK03918

DNA double-strand break repair ATPase Rad50;

102-343

7.05e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.05e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  102 YQERLARLENDKESLVLQVSVLTDQV---EAQGEKIRDLEFCLEEHREKLNATEEMLQQellsrtsLETQKlDLMAEISN 178
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL-------YEEAK-AKKEELER 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  179 LKLKLTAVEKDRLDyedkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKV---GQMQYEKQRM 255
Cdd:PRK03918   377 LKKRLTGLTPEKLE-----KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRK 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462535194  256 EQKwESLKDELASLKEQL---EEKESEVKRLQEKLVCKMKGEGVEIVDRDIeVQKMKKAVESLMAAN----EEKDRKIED 328
Cdd:PRK03918   452 ELL-EEYTAELKRIEKELkeiEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNleelEKKAEEYEK 529

                          250
                   ....*....|....*
gi 2462535194  329 LRQCLNRYKKMQDTV 343
Cdd:PRK03918   530 LKEKLIKLKGEIKSL 544

Myosin_tail_1