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Conserved domains on  [gi|1907076625|ref|XP_036011828|]
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nesprin-1 isoform X26 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
24-143 7.18e-71

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409090  Cd Length: 113  Bit Score: 233.81  E-value: 7.18e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21241     81 -------IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
182-290 1.49e-70

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409092  Cd Length: 109  Bit Score: 232.98  E-value: 1.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21243      1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                           90       100
                   ....*....|....*....|....*....
gi 1907076625  262 LLDPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21243     81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4967-5802 6.00e-11

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 6.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4967 LEHTLAELQELDgDVQEALRTRQATLTEIYSRCQRYYQvfqaandwLDDAQEMLQLAGNGLDVESAEENLRshmEFFKTE 5046
Cdd:TIGR02168  181 LERTRENLDRLE-DILNELERQLKSLERQAEKAERYKE--------LKAELRELELALLVLRLEELREELE---ELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5047 GQFHSNMEELRGLVARLDPLIkatgkEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVielmNDAEK 5126
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKL-----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL----ERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5127 KLSEFAVLKTSSIHEAEEKLskhKALVSVVDSFHEKIVALEEKASQLEQTgndtsKATLSRSMTTVWQRWTRLR-AVAQD 5205
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEELEAE-----LEELESRLEELEEQLETLRsKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5206 QEKI------LEDAVDEWKRLSAKVKETTEVINQLQGRLpgsstEKASKAELMTLLESHDTYLMDLESQQLTLgvlqQRA 5279
Cdd:TIGR02168  392 ELQIaslnneIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQAELEELEEELEELQEELERL----EEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5280 LSMLQDRAFPGTEEEVPI---LRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYlgnpTIE 5356
Cdd:TIGR02168  463 LEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY----EAA 538
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5357 IDTQLEElkRLLAEATSHQESIEKIAEEQKNKYLGLYTVLP-------------SEISLQLAEVALDLKIHDQIQEK--- 5420
Cdd:TIGR02168  539 IEAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndREILKNIEGFLGVAKDLVKFDPKlrk 616
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5421 -----------VQEIEEGKAMSQEFSCKIQKVTKDLTTI-----LTKLKAKTDD-LVHAKAEHKMLGEELDGCNSKLMEL 5483
Cdd:TIGR02168  617 alsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvITGGSAKTNSsILERRREIEELEEKIEELEEKIAEL 696
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5484 DAAIQTFSERHSQLGQPLAKKIGKLTEL-------------HQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKA 5550
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELsrqisalrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5551 KVLVHGNIAwnsasQLQEQYilhQTLLEESGEIDSDLEAMAEKVQHLANVYctGKLSQQVTQFGREMEELRQAIRVRLRN 5630
Cdd:TIGR02168  777 LAEAEAEIE-----ELEAQI---EQLKEELKALREALDELRAELTLLNEEA--ANLRERLESLERRIAATERRLEDLEEQ 846
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5631 LQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLchrQHLLSEMESLKPKMQAVQLCQSALRipedvvasl 5710
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSELR--------- 914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5711 plcHAALRLQEEASQLQhtaiqqcnimqeavVQYEQYKQEMKHLQQLIEEAHREIEDKPVATSNIQELQAqislhEELAQ 5790
Cdd:TIGR02168  915 ---RELEELREKLAQLE--------------LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE-----EEARR 972
                          890
                   ....*....|..
gi 1907076625 5791 KIKGYQEQIDSL 5802
Cdd:TIGR02168  973 RLKRLENKIKEL 984
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3821-4011 3.11e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 63.62  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3821 LAKEFSDKYKVLAQWMAEyQEILCTPEEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQS--LKD 3898
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3899 KIQKLQSDFQDLCSRAKERVFSLEAKVKDHEdYNTELQEVEKWLLQMSGRLVAPDLLEmsSLETITQQLAHHKAMMEEIA 3978
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELE 156
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907076625 3979 GFEDRLDNLKAKGDTLIGQCPEHLQAKQKQTVQ 4011
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1167-2008 3.59e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 3.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1167 DEVKHMVDEIRNDITKKGESLSWLKSRLkylidisseneaQKRGDELAELSSSFKALVALLSEVEkllsnfgecvQYKEI 1246
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEV------------SELEEEIEELQKELYALANEISRLE----------QQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1247 VKSSLEGLisgpQESKEEAEMILDsknllEAQQLLLHHQQKTKMISAKKRDLQEQMEQAQQGGQAGPgqEELRKLESTLT 1326
Cdd:TIGR02168  307 LRERLANL----ERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELE--AELEELESRLE 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1327 GLEQSRERQERRIqVSLRkwERFETNKETVVRYLFQTGSSHERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKE 1406
Cdd:TIGR02168  376 ELEEQLETLRSKV-AQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1407 AAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTMEMVKSKWDHFGSNFETLSIWILEKEnelssleASASAADVQ 1486
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS-------GLSGILGVL 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1487 ISQIKVTiQEIESKIDsiVGLEEEAQSFaqfVTTGESARIKAkltqirryWEELQEHARGLEGTILGHLSQQQKFEENLR 1566
Cdd:TIGR02168  526 SELISVD-EGYEAAIE--AALGGRLQAV---VVENLNAAKKA--------IAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1567 KIRQSVSEFAERLADPIKIcssAAETYKVLQEHMDLCQAVESLSST-------------VT-----------MFSASAQK 1622
Cdd:TIGR02168  592 EILKNIEGFLGVAKDLVKF---DPKLRKALSYLLGGVLVVDDLDNAlelakklrpgyriVTldgdlvrpggvITGGSAKT 668
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1623 AVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQL 1702
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1703 IQALQNEVVSQASLYSNLLQLKEALFS--VASKEDVAVMKLQLEQLDERWGDLPQIISkrmhflqsvlAEHKQFDELlfs 1780
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALD----------ELRAELTLL--- 815
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1781 fsvwiKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAqdlhpLQSKVDDCFQLFEEA 1860
Cdd:TIGR02168  816 -----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASL 885
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1861 SQVVERRKLALAQLAEFLQSHACMSTLLYQLRQtvEATKSMSKkqsdsLKTDLHSAIQDVKTLESSAISLDGTLTKAQCH 1940
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 1941 LKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEE---RMDRE 2008
Cdd:TIGR02168  959 LENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEaieEIDRE 1029
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3394-3599 3.90e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.46  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3394 KWTSYQDDVRQFSSWMDSVEVSL--TESEKQHTELREKITalgKAKLLNEEVLSHSSLLETIEVKRAAMTEHY-----VT 3466
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLssTDYGDDLESVEALLK---KHEALEAELAAHEERVEALNELGEQLIEEGhpdaeEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3467 QLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYqRDLKAFESWLEQEQEKLDRcSVHEGDTNAHETMLRDLQELQVRC 3546
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907076625 3547 AEGQALLNSVLHTREDVIPSGLPQAEDRV---LESLRQDWQVYQHRLAEARMQLNN 3599
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEE 211
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3091-3661 7.08e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 7.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3091 TAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLNTMLFKGELlSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKES 3170
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3171 ALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNRLYDLPAK----RREQQKLQSVLEEiQCYEPQLHRLKEKARQLWE 3246
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEE-LLKKLEEAELKELQAELEE 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3247 GQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEHNRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLK 3326
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3327 LEALLSVRQEKEIQMkmvvtrgEYVLQSTSLegsAAVQQQLQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFS 3406
Cdd:TIGR02168  525 LSELISVDEGYEAAI-------EAALGGRLQ---AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3407 SWMDSVEVSLTESEKQHTELREKI--------------TALGKAKLLNEE---------------------------VLS 3445
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILE 674
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3446 HSSLLETIEVKRAAMTEHY-VTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSV 3524
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3525 HEGDTNAHETMLRD----LQELQVRCAEGQALLNSVLHTREDVIpsglpQAEDRVLESLRQDWQVYQHRLAEARMQLNNV 3600
Cdd:TIGR02168  755 ELTELEAEIEELEErleeAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 3601 VNKLRLMEQKFQQADEWLKRMEEKInfrSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEE 3661
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERASLEE 887
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3927-4153 1.03e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 56.30  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3927 DHEDYNTELQEVEKWLLQMSGRLVAPDLLemSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHlqakq 4006
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4007 KQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDtLQQCQAWISAVQPDLKpSPQPPLSRAEAVKQVKHFRAL 4086
Cdd:cd00176     74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4087 QEQARTYLDLLCSMCDLSNSSVKNtakdiqQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDA 4153
Cdd:cd00176    152 EEELEAHEPRLKSLNELAEELLEE------GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2281-3120 2.44e-07

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2281 IEADLRQKLEHAKEITEEARGTLKdFTAQRtqverfvkditawlinvEESLTRCAQTEtcEGLKKAKDIRKELQSQQNSI 2360
Cdd:TIGR02168  146 ISEIIEAKPEERRAIFEEAAGISK-YKERR-----------------KETERKLERTR--ENLDRLEDILNELERQLKSL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2361 TST----------QEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQARIQDSLEKH-----FSGSMKEFQEW 2425
Cdd:TIGR02168  206 ERQaekaerykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlEVSELEEEIEE 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2426 FLGA-KAAARESSNLTGDSQILEARLHNLQGVLDSLSD----GQSKLDVVtqegqtlyahlpKQIVSSIQEQITKANEEF 2500
Cdd:TIGR02168  286 LQKElYALANEISRLEQQKQILRERLANLERQLEELEAqleeLESKLDEL------------AEELAELEEKLEELKEEL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2501 QAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTEN--LGESKHHISEKKNEVRKVEMFLGELLAARESL 2578
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2579 DKLSQRGQL--LSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKDVQDRLACAes 2656
Cdd:TIGR02168  434 ELKELQAELeeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL-- 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2657 tLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLE---------MLKKAWAEAMNSAVH 2727
Cdd:TIGR02168  512 -LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKqnelgrvtfLPLDSIKGTEIQGND 590
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2728 AQS--TLESVIDQWNDYLEKKSQLEQWMES------VDQRLEHPLQLQPGLKEKFSL--LDHFQ-----SIVSEAEDHTG 2792
Cdd:TIGR02168  591 REIlkNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKKLRPGYRIvtLDGDLvrpggVITGGSAKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2793 ALQQLAAKSRELYQK----TQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKD-HLMYLDavqefadwLHSAKEEL 2867
Cdd:TIGR02168  671 SILERRREIEELEEKieelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKD--------LARLEAEV 742
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2868 HRWSDTSGDPSATQKKLLKIKELIDSREIGA-GRLSRVESLAPAVKQ--NTAASGCELLNSEMQALRADWRQWEDCLFQT 2944
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAeEELAEAEAEIEELEAqiEQLKEELKALREALDELRAELTLLNEEAANL 822
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2945 QSSLESLVSEMALSEQEFfgqvTQLEQALEQFctllktwAQQLTLLEGknsdeEILECWHKGREILDALQKA----EPMT 3020
Cdd:TIGR02168  823 RERLESLERRIAATERRL----EDLEEQIEEL-------SEDIESLAA-----EIEELEELIEELESELEALlnerASLE 886
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3021 EDLKSQLNELCRFSRDLSPYSEKVSGLIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKittakcfDLPQN 3100
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE-------EAEAL 959
                          890       900
                   ....*....|....*....|
gi 1907076625 3101 LSEVSSSLQKIQEFLSESEN 3120
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLEN 979
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4349-4565 2.63e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4349 ELNVIQSRFQELMEWAEEQQpNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLKSLMKDADRvMADLGLNERKVIQ 4428
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4429 KALSEAQKHVSCLSDLVGQRRKYLNKALsEKTQFLMAVFQATSQIQQHERKIVfREYICLLPDDVSKQVKTCKTAQASLK 4508
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4509 TYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSL 4565
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
753-1006 3.56e-04

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  753 QDLEDLEKRVPVMDAQYKmiAKKAHLFAKESPQEEANEMLTTM-----------SKLKEQLSKVKECCSPLLYEAQQLTV 821
Cdd:TIGR02168  677 REIEELEEKIEELEEKIA--ELEKALAELRKELEELEEELEQLrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  822 PLEELETQITSFYDSLGKINEILSVLEQEAqsstlfkqkhQELLASQENCKKSLTLIEKGSQSVQKLVTS---SQARKPW 898
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEI----------EELEAQIEQLKEELKALREALDELRAELTLlneEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  899 DHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAqegLEEKGDPEELLRRHTEFFSQLDQ 978
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907076625  979 RV------LNAFLKACDELTDILpEQEQQGLQEA 1006
Cdd:TIGR02168  902 ELreleskRSELRRELEELREKL-AQLELRLEGL 934
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4490-4666 1.38e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4490 PDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGiTKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLVSRK 4569
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4570 HFkEDFDKACHWLKQADIVTFPEiNLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLSEKL 4649
Cdd:cd00176    111 FF-RDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
                          170
                   ....*....|....*..
gi 1907076625 4650 SALPQQFNVIVALAKDK 4666
Cdd:cd00176    189 EELNERWEELLELAEER 205
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4144-4341 1.70e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4144 AELWIYLQDADQQLQNMKRRHTELEIniaQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKN--QESPEHKE-ITHLND 4220
Cdd:cd00176     10 DELEAWLSEKEELLSSTDYGDDLESV---EALLKKHEALEAELAAHEERVEALNELGEQLIEEghPDAEEIQErLEELNQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4221 QWQDLClqsdKLCAQREQDLQRTSSYHDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYA----I 4296
Cdd:cd00176     87 RWEELR----ELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAheprL 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907076625 4297 DDLKDCKQKLIEQLGLDDRELVREQTSHLEQRWFQLQDLVKRKIQ 4341
Cdd:cd00176    163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1983-2200 1.97e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1983 LKEAFREQKEELLRSIEDIEERMDRERLkVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDR 2062
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2063 EINGLEATWDDTRRQIHENQGQCCGLIDLVREYQSLKStVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSK 2142
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907076625 2143 QKELDSFTSKGKHLLSELkkiHSGDFSLVKTDMESTLDKWLDVSERIEENMDMLRVSL 2200
Cdd:cd00176    159 EPRLKSLNELAEELLEEG---HPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
Name Accession Description Interval E-value
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
24-143 7.18e-71

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 233.81  E-value: 7.18e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21241     81 -------IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
182-290 1.49e-70

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 232.98  E-value: 1.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21243      1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                           90       100
                   ....*....|....*....|....*....
gi 1907076625  262 LLDPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21243     81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
24-283 1.19e-29

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.91  E-value: 1.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:COG5069      5 KWQKVQKKTFTKWTNEKLISGGQKEF-GDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEeltsnlpqlqslsssassvdsmvstetasppskrKVAAKI 183
Cdd:COG5069     84 -------VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA----------------------------------TINEEG 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQH-TAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKV-KTRSNRE-NLEDAFTIAETQLGIP 260
Cdd:COG5069    123 ELTKHINLLLWCDEdTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIA 202
                          250       260
                   ....*....|....*....|....
gi 1907076625  261 RLLDPEDV-DVDKPDEKSIMTYVA 283
Cdd:COG5069    203 RLIGVEDIvNVSIPDERSIMTYVS 226
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
187-285 2.29e-21

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.35  E-value: 2.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQ-HTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTR--SNRENLEDAFTIAETQLGIPR-L 262
Cdd:pfam00307    3 LEKELLRWINsHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|...
gi 1907076625  263 LDPEdvDVDKPDEKSIMTYVAQF 285
Cdd:pfam00307   83 IEPE--DLVEGDNKSVLTYLASL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
28-142 1.15e-18

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 84.65  E-value: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPcEQGHRVKRIHAVANIGTALKFLEgrKSMyr 107
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-KKKLNKSEFDKLENINLALDVAE--KKL-- 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907076625  108 gsPIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:pfam00307   77 --GVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
189-285 5.27e-15

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.89  E-value: 5.27e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   189 KTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNR----ENLEDAFTIAETQLGIPRLLD 264
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1907076625   265 PEDVDVDKPDEKSIMTYVAQF 285
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
31-139 1.64e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.65  E-value: 1.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625    31 RTFTKWINSHLAKRKPPmVVDDLFEDMKDGIKLLALLEVLSGQKLPceqgHRVK-----RIHAVANIGTALKFLEGRKsm 105
Cdd:smart00033    1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVD----KKKVaaslsRFKKIENINLALSFAEKLG-- 73
                            90       100       110
                    ....*....|....*....|....*....|....
gi 1907076625   106 yrgspIKLVNINATDIADGRPSIvLGLMWTIILY 139
Cdd:smart00033   74 -----GKVVLFEPEDLVEGPKLI-LGVIWTLISL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4967-5802 6.00e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 6.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4967 LEHTLAELQELDgDVQEALRTRQATLTEIYSRCQRYYQvfqaandwLDDAQEMLQLAGNGLDVESAEENLRshmEFFKTE 5046
Cdd:TIGR02168  181 LERTRENLDRLE-DILNELERQLKSLERQAEKAERYKE--------LKAELRELELALLVLRLEELREELE---ELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5047 GQFHSNMEELRGLVARLDPLIkatgkEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVielmNDAEK 5126
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKL-----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL----ERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5127 KLSEFAVLKTSSIHEAEEKLskhKALVSVVDSFHEKIVALEEKASQLEQTgndtsKATLSRSMTTVWQRWTRLR-AVAQD 5205
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEELEAE-----LEELESRLEELEEQLETLRsKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5206 QEKI------LEDAVDEWKRLSAKVKETTEVINQLQGRLpgsstEKASKAELMTLLESHDTYLMDLESQQLTLgvlqQRA 5279
Cdd:TIGR02168  392 ELQIaslnneIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQAELEELEEELEELQEELERL----EEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5280 LSMLQDRAFPGTEEEVPI---LRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYlgnpTIE 5356
Cdd:TIGR02168  463 LEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY----EAA 538
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5357 IDTQLEElkRLLAEATSHQESIEKIAEEQKNKYLGLYTVLP-------------SEISLQLAEVALDLKIHDQIQEK--- 5420
Cdd:TIGR02168  539 IEAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndREILKNIEGFLGVAKDLVKFDPKlrk 616
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5421 -----------VQEIEEGKAMSQEFSCKIQKVTKDLTTI-----LTKLKAKTDD-LVHAKAEHKMLGEELDGCNSKLMEL 5483
Cdd:TIGR02168  617 alsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvITGGSAKTNSsILERRREIEELEEKIEELEEKIAEL 696
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5484 DAAIQTFSERHSQLGQPLAKKIGKLTEL-------------HQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKA 5550
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELsrqisalrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5551 KVLVHGNIAwnsasQLQEQYilhQTLLEESGEIDSDLEAMAEKVQHLANVYctGKLSQQVTQFGREMEELRQAIRVRLRN 5630
Cdd:TIGR02168  777 LAEAEAEIE-----ELEAQI---EQLKEELKALREALDELRAELTLLNEEA--ANLRERLESLERRIAATERRLEDLEEQ 846
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5631 LQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLchrQHLLSEMESLKPKMQAVQLCQSALRipedvvasl 5710
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSELR--------- 914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5711 plcHAALRLQEEASQLQhtaiqqcnimqeavVQYEQYKQEMKHLQQLIEEAHREIEDKPVATSNIQELQAqislhEELAQ 5790
Cdd:TIGR02168  915 ---RELEELREKLAQLE--------------LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE-----EEARR 972
                          890
                   ....*....|..
gi 1907076625 5791 KIKGYQEQIDSL 5802
Cdd:TIGR02168  973 RLKRLENKIKEL 984
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5000-5213 2.91e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 63.62  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5000 QRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTEGQFHSNMEELRGLVARLDPLiKATGKEELAQKM 5079
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5080 ASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREgVIELMNDAEKKLSefAVLKTSSIHEAEEKLSKHKALVSVVDSF 5159
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907076625 5160 HEKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQEKILEDA 5213
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3821-4011 3.11e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 63.62  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3821 LAKEFSDKYKVLAQWMAEyQEILCTPEEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQS--LKD 3898
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3899 KIQKLQSDFQDLCSRAKERVFSLEAKVKDHEdYNTELQEVEKWLLQMSGRLVAPDLLEmsSLETITQQLAHHKAMMEEIA 3978
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELE 156
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907076625 3979 GFEDRLDNLKAKGDTLIGQCPEHLQAKQKQTVQ 4011
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1167-2008 3.59e-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: 63.92  E-value: 3.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1167 DEVKHMVDEIRNDITKKGESLSWLKSRLkylidisseneaQKRGDELAELSSSFKALVALLSEVEkllsnfgecvQYKEI 1246
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEV------------SELEEEIEELQKELYALANEISRLE----------QQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1247 VKSSLEGLisgpQESKEEAEMILDsknllEAQQLLLHHQQKTKMISAKKRDLQEQMEQAQQGGQAGPgqEELRKLESTLT 1326
Cdd:TIGR02168  307 LRERLANL----ERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELE--AELEELESRLE 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1327 GLEQSRERQERRIqVSLRkwERFETNKETVVRYLFQTGSSHERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKE 1406
Cdd:TIGR02168  376 ELEEQLETLRSKV-AQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1407 AAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTMEMVKSKWDHFGSNFETLSIWILEKEnelssleASASAADVQ 1486
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS-------GLSGILGVL 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1487 ISQIKVTiQEIESKIDsiVGLEEEAQSFaqfVTTGESARIKAkltqirryWEELQEHARGLEGTILGHLSQQQKFEENLR 1566
Cdd:TIGR02168  526 SELISVD-EGYEAAIE--AALGGRLQAV---VVENLNAAKKA--------IAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1567 KIRQSVSEFAERLADPIKIcssAAETYKVLQEHMDLCQAVESLSST-------------VT-----------MFSASAQK 1622
Cdd:TIGR02168  592 EILKNIEGFLGVAKDLVKF---DPKLRKALSYLLGGVLVVDDLDNAlelakklrpgyriVTldgdlvrpggvITGGSAKT 668
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1623 AVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQL 1702
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1703 IQALQNEVVSQASLYSNLLQLKEALFS--VASKEDVAVMKLQLEQLDERWGDLPQIISkrmhflqsvlAEHKQFDELlfs 1780
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALD----------ELRAELTLL--- 815
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1781 fsvwiKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAqdlhpLQSKVDDCFQLFEEA 1860
Cdd:TIGR02168  816 -----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASL 885
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1861 SQVVERRKLALAQLAEFLQSHACMSTLLYQLRQtvEATKSMSKkqsdsLKTDLHSAIQDVKTLESSAISLDGTLTKAQCH 1940
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 1941 LKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEE---RMDRE 2008
Cdd:TIGR02168  959 LENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEaieEIDRE 1029
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3394-3599 3.90e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.46  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3394 KWTSYQDDVRQFSSWMDSVEVSL--TESEKQHTELREKITalgKAKLLNEEVLSHSSLLETIEVKRAAMTEHY-----VT 3466
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLssTDYGDDLESVEALLK---KHEALEAELAAHEERVEALNELGEQLIEEGhpdaeEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3467 QLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYqRDLKAFESWLEQEQEKLDRcSVHEGDTNAHETMLRDLQELQVRC 3546
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907076625 3547 AEGQALLNSVLHTREDVIPSGLPQAEDRV---LESLRQDWQVYQHRLAEARMQLNN 3599
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEE 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3091-3661 7.08e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 7.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3091 TAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLNTMLFKGELlSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKES 3170
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3171 ALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNRLYDLPAK----RREQQKLQSVLEEiQCYEPQLHRLKEKARQLWE 3246
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEE-LLKKLEEAELKELQAELEE 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3247 GQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEHNRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLK 3326
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3327 LEALLSVRQEKEIQMkmvvtrgEYVLQSTSLegsAAVQQQLQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFS 3406
Cdd:TIGR02168  525 LSELISVDEGYEAAI-------EAALGGRLQ---AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3407 SWMDSVEVSLTESEKQHTELREKI--------------TALGKAKLLNEE---------------------------VLS 3445
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILE 674
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3446 HSSLLETIEVKRAAMTEHY-VTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSV 3524
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3525 HEGDTNAHETMLRD----LQELQVRCAEGQALLNSVLHTREDVIpsglpQAEDRVLESLRQDWQVYQHRLAEARMQLNNV 3600
Cdd:TIGR02168  755 ELTELEAEIEELEErleeAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 3601 VNKLRLMEQKFQQADEWLKRMEEKInfrSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEE 3661
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERASLEE 887
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3927-4153 1.03e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 56.30  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3927 DHEDYNTELQEVEKWLLQMSGRLVAPDLLemSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHlqakq 4006
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4007 KQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDtLQQCQAWISAVQPDLKpSPQPPLSRAEAVKQVKHFRAL 4086
Cdd:cd00176     74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4087 QEQARTYLDLLCSMCDLSNSSVKNtakdiqQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDA 4153
Cdd:cd00176    152 EEELEAHEPRLKSLNELAEELLEE------GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3181-3392 1.82e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 55.53  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3181 DFEVSAELVQNWLSKTERLVQeSSNRLYDLPAKRREQQKLQSVLEEIQCYEPQLHRLKEKARQLWEGQAASKSFVH-RVS 3259
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQeRLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3260 QLSSQYLALSNVTKEKVSRLDRIIAEHnRFSQGVKELQDWMSDAVHMLDSYcLPTSDKSVLDSRMLKLEALLSVRQEKEI 3339
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 3340 QMKMVVTRGEYVLQSTSLEGSAAVQQQLQAVKDMWESLLSAAIRCKSQLEGAL 3392
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2281-3120 2.44e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2281 IEADLRQKLEHAKEITEEARGTLKdFTAQRtqverfvkditawlinvEESLTRCAQTEtcEGLKKAKDIRKELQSQQNSI 2360
Cdd:TIGR02168  146 ISEIIEAKPEERRAIFEEAAGISK-YKERR-----------------KETERKLERTR--ENLDRLEDILNELERQLKSL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2361 TST----------QEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQARIQDSLEKH-----FSGSMKEFQEW 2425
Cdd:TIGR02168  206 ERQaekaerykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlEVSELEEEIEE 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2426 FLGA-KAAARESSNLTGDSQILEARLHNLQGVLDSLSD----GQSKLDVVtqegqtlyahlpKQIVSSIQEQITKANEEF 2500
Cdd:TIGR02168  286 LQKElYALANEISRLEQQKQILRERLANLERQLEELEAqleeLESKLDEL------------AEELAELEEKLEELKEEL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2501 QAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTEN--LGESKHHISEKKNEVRKVEMFLGELLAARESL 2578
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2579 DKLSQRGQL--LSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKDVQDRLACAes 2656
Cdd:TIGR02168  434 ELKELQAELeeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL-- 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2657 tLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLE---------MLKKAWAEAMNSAVH 2727
Cdd:TIGR02168  512 -LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKqnelgrvtfLPLDSIKGTEIQGND 590
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2728 AQS--TLESVIDQWNDYLEKKSQLEQWMES------VDQRLEHPLQLQPGLKEKFSL--LDHFQ-----SIVSEAEDHTG 2792
Cdd:TIGR02168  591 REIlkNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKKLRPGYRIvtLDGDLvrpggVITGGSAKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2793 ALQQLAAKSRELYQK----TQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKD-HLMYLDavqefadwLHSAKEEL 2867
Cdd:TIGR02168  671 SILERRREIEELEEKieelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKD--------LARLEAEV 742
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2868 HRWSDTSGDPSATQKKLLKIKELIDSREIGA-GRLSRVESLAPAVKQ--NTAASGCELLNSEMQALRADWRQWEDCLFQT 2944
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAeEELAEAEAEIEELEAqiEQLKEELKALREALDELRAELTLLNEEAANL 822
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2945 QSSLESLVSEMALSEQEFfgqvTQLEQALEQFctllktwAQQLTLLEGknsdeEILECWHKGREILDALQKA----EPMT 3020
Cdd:TIGR02168  823 RERLESLERRIAATERRL----EDLEEQIEEL-------SEDIESLAA-----EIEELEELIEELESELEALlnerASLE 886
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3021 EDLKSQLNELCRFSRDLSPYSEKVSGLIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKittakcfDLPQN 3100
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE-------EAEAL 959
                          890       900
                   ....*....|....*....|
gi 1907076625 3101 LSEVSSSLQKIQEFLSESEN 3120
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLEN 979
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1660-1873 2.37e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1660 RWQRLEKGLSPFLTWLERCEAIASSPekDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALfSVASKEDVAVM 1739
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1740 KLQLEQLDERWGDLPQIISKRMHFLQSVLAEHKQFDELLfSFSVWIKQFLGELQRTSEI-NLRDHQVALTRHKDHAAEIE 1818
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907076625 1819 KKRGEITHLQGHLSQLRSLGRAQDLHPLQSKVDDCFQLFEEASQVVERRKLALAQ 1873
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4349-4565 2.63e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4349 ELNVIQSRFQELMEWAEEQQpNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLKSLMKDADRvMADLGLNERKVIQ 4428
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4429 KALSEAQKHVSCLSDLVGQRRKYLNKALsEKTQFLMAVFQATSQIQQHERKIVfREYICLLPDDVSKQVKTCKTAQASLK 4508
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4509 TYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSL 4565
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1494-2078 3.08e-06

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: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1494 IQEIESKIDSivgLEEEAQSFAQFVTTGESARIK------AKLTQIRRYWEELQEHARGLEGTILGHLSQQQKFEENLRK 1567
Cdd:COG1196    195 LGELERQLEP---LERQAEKAERYRELKEELKELeaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1568 IRQSVSEFAERLADpikicsSAAETYKVLQEHMDLCQAVESLSSTVTMFSASAQKAVNR--------ESCTQEAAALQQQ 1639
Cdd:COG1196    272 LRLELEELELELEE------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleeelEELEEELEELEEE 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1640 YEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQLIQALQNEvvsQASLYSN 1719
Cdd:COG1196    346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEE 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1720 LLQLKEALFSVASKEDVAVMKLQLEQLDERwgdlpQIISKRMHFLQSVLAEHKQFDELLfsfSVWIKQFLGELQRTSEIN 1799
Cdd:COG1196    423 LEELEEALAELEEEEEEEEEALEEAAEEEA-----ELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLL 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1800 LRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAQDLHP-------LQSKVDDcfqLFEEASQVVERRKLALA 1872
Cdd:COG1196    495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaaLQNIVVE---DDEVAAAAIEYLKAAKA 571
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1873 QLAEFLQSHAcMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESSAISLDGTLTKAQCHLKSASPEERTSC 1952
Cdd:COG1196    572 GRATFLPLDK-IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1953 RATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMDRERLKVPTRQALQHRLRVFNQLEDEL 2032
Cdd:COG1196    651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1907076625 2033 NSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRRQI 2078
Cdd:COG1196    731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2414-2619 5.90e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2414 HFSGSMKEFQEWfLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQSKLDVVTQEGQTLYAHLPKQIvSSIQEQI 2493
Cdd:cd00176      4 QFLRDADELEAW-LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2494 TKANEEFQAFLKQCLKEKQALQDCVSELGSFEDqHRKLNLWIHEMEERLKTENLGESKHHISEKkneVRKVEMFLGELLA 2573
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEEL---LKKHKELEEELEA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907076625 2574 ARESLDKLSQRGQLLSEESHSAGKGGCRST--QLLTSYQSLLRVTKEK 2619
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKleELNERWEELLELAEER 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
753-1006 3.56e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  753 QDLEDLEKRVPVMDAQYKmiAKKAHLFAKESPQEEANEMLTTM-----------SKLKEQLSKVKECCSPLLYEAQQLTV 821
Cdd:TIGR02168  677 REIEELEEKIEELEEKIA--ELEKALAELRKELEELEEELEQLrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  822 PLEELETQITSFYDSLGKINEILSVLEQEAqsstlfkqkhQELLASQENCKKSLTLIEKGSQSVQKLVTS---SQARKPW 898
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEI----------EELEAQIEQLKEELKALREALDELRAELTLlneEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  899 DHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAqegLEEKGDPEELLRRHTEFFSQLDQ 978
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907076625  979 RV------LNAFLKACDELTDILpEQEQQGLQEA 1006
Cdd:TIGR02168  902 ELreleskRSELRRELEELREKL-AQLELRLEGL 934
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3394-3672 5.38e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3394 KWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALgkakllneevlshSSLLETIEVKRAAMTEhyvtqlELQDL 3473
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL-------------EEKLEELRLEVSELEE------EIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3474 QERHQALKEKakeaVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRcsvHEGDTNAHETMLRD-LQELQVRCAEGQAL 3552
Cdd:TIGR02168  287 QKELYALANE----ISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEkLEELKEELESLEAE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3553 LNSVLHTREDvipsglpqAEDRvLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEKINFRSECQ 3632
Cdd:TIGR02168  360 LEELEAELEE--------LESR-LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907076625 3633 SSRSDKEIQ--LLQLKKWHEDLSAHRDEVEEVGTRAQGILDE 3672
Cdd:TIGR02168  431 EEAELKELQaeLEELEEELEELQEELERLEEALEELREELEE 472
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4490-4666 1.38e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4490 PDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGiTKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLVSRK 4569
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4570 HFkEDFDKACHWLKQADIVTFPEiNLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLSEKL 4649
Cdd:cd00176    111 FF-RDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
                          170
                   ....*....|....*..
gi 1907076625 4650 SALPQQFNVIVALAKDK 4666
Cdd:cd00176    189 EELNERWEELLELAEER 205
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4144-4341 1.70e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4144 AELWIYLQDADQQLQNMKRRHTELEIniaQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKN--QESPEHKE-ITHLND 4220
Cdd:cd00176     10 DELEAWLSEKEELLSSTDYGDDLESV---EALLKKHEALEAELAAHEERVEALNELGEQLIEEghPDAEEIQErLEELNQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4221 QWQDLClqsdKLCAQREQDLQRTSSYHDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYA----I 4296
Cdd:cd00176     87 RWEELR----ELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAheprL 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907076625 4297 DDLKDCKQKLIEQLGLDDRELVREQTSHLEQRWFQLQDLVKRKIQ 4341
Cdd:cd00176    163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4143-4439 1.90e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4143 KAELWIYL---QDADQQLQNMKRRHTELEINIAQNMVmQVKDFIKQLQCKQVSVSTIVEKVDKLTKNQESPEHKEITHLN 4219
Cdd:TIGR02169  222 EYEGYELLkekEALERQKEAIERQLASLEEELEKLTE-EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4220 DQwQDLCLQSDKLCAQREQDLQRTSsyhdhmRVVEAFLEKFTTEWDSLARSnaestaihLEALKKLALALQEEmyaIDDL 4299
Cdd:TIGR02169  301 AE-IASLERSIAEKERELEDAEERL------AKLEAEIDKLLAEIEELERE--------IEEERKRRDKLTEE---YAEL 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4300 KDCKQKLIEQLGLDDRELvreqtshleQRWFQLQDLVKRKIQVSVTNLEELNVIQSRFQELMEWAEEQQPNIVEALKQsp 4379
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEF---------AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG-- 431
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 4380 ppgmaqhLLMDHLAICSELEAKQVLLKSLMKDADRVMADLGLNERKV---------IQKALSEAQKHVS 4439
Cdd:TIGR02169  432 -------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlkeeydrVEKELSKLQRELA 493
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1983-2200 1.97e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1983 LKEAFREQKEELLRSIEDIEERMDRERLkVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDR 2062
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2063 EINGLEATWDDTRRQIHENQGQCCGLIDLVREYQSLKStVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSK 2142
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907076625 2143 QKELDSFTSKGKHLLSELkkiHSGDFSLVKTDMESTLDKWLDVSERIEENMDMLRVSL 2200
Cdd:cd00176    159 EPRLKSLNELAEELLEEG---HPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PLN02939 PLN02939
transferase, transferring glycosyl groups
2627-2871 2.22e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.89  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2627 LKEHEALEEATQSMWARVKDVQDRLACAESTLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNkegqQA 2706
Cdd:PLN02939   162 LTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEN----ML 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2707 IQDQLEMLKKawaeamnSAVHAQSTLESVIdqwndYLEK-KSQLEQWMESVDQRL----EHPLQLQP----GLKEKFSLL 2777
Cdd:PLN02939   238 LKDDIQFLKA-------ELIEVAETEERVF-----KLEKeRSLLDASLRELESKFivaqEDVSKLSPlqydCWWEKVENL 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2778 DH-FQSIVSEAEDHTGALQQlaakSRELYQKTQ--DESFKEAGQEELRTQFQDIMtvaKEKMRTVEDLVK--DHLM---- 2848
Cdd:PLN02939   306 QDlLDRATNQVEKAALVLDQ----NQDLRDKVDklEASLKEANVSKFSSYKVELL---QQKLKLLEERLQasDHEIhsyi 378
                          250       260
                   ....*....|....*....|....*
gi 1907076625 2849 --YLDAVQEFADWLHSAKEELHRWS 2871
Cdd:PLN02939   379 qlYQESIKEFQDTLSKLKEESKKRS 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3469-3666 2.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3469 ELQDLQERHQALkEKAKEAVTKLEKLVRLHQEYQRdlkafeswLEQEQEKLDRCsvheGDTNAHETMLRDLQELQVRCAE 3548
Cdd:COG4913    233 HFDDLERAHEAL-EDAREQIELLEPIRELAERYAA--------ARERLAELEYL----RAALRLWFAQRRLELLEAELEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3549 GQALLNSvLHTREDVIPSGLPQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEKINfr 3628
Cdd:COG4913    300 LRAELAR-LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP-- 376
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907076625 3629 secqSSRSDKEIQLLQLKKWHEDLSAHRDEVEEVGTRA 3666
Cdd:COG4913    377 ----ASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
SPEC smart00150
Spectrin repeats;
3929-4036 2.71e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 2.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  3929 EDYNTELQEVEKWLLQMSGRLVAPDLleMSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHlqakqKQ 4008
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDL--GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-----AE 73
                            90       100
                    ....*....|....*....|....*...
gi 1907076625  4009 TVQAHLQGTKDSYSAICSTAQRVYRSLE 4036
Cdd:smart00150   74 EIEERLEELNERWEELKELAEERRQKLE 101
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
5109-5549 2.99e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5109 EYQKAREGVIELMNDAEKKLSEFAVLKtssIHEAEEKLSKHKALvsvvDSFHEKIVALEEkasQLEQTGNDTSKaTLSRS 5188
Cdd:pfam05483  177 EREETRQVYMDLNNNIEKMILAFEELR---VQAENARLEMHFKL----KEDHEKIQHLEE---EYKKEINDKEK-QVSLL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5189 MTTVWQRWTRLRavaqDQEKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTE-KASKAELMTLLESHDTYLMDLES 5267
Cdd:pfam05483  246 LIQITEKENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKElEDIKMSLQRSMSTQKALEEDLQI 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5268 QQLTLGVLQQRALSMLQDRAFPGTEEEVpilrAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETK 5347
Cdd:pfam05483  322 ATKTICQLTEEKEAQMEELNKAKAAHSF----VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5348 DYLGNPTIEidtqLEELKRLLAEATS---HQESIEKIAEEQKNKYLGLYTVLPS------EISLQLAEVALDLKIH-DQI 5417
Cdd:pfam05483  398 KFKNNKEVE----LEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKTSEEHYlKEV 473
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5418 QEKVQEIEEGK-------AMSQEFSCKIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTF 5490
Cdd:pfam05483  474 EDLKTELEKEKlknieltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 5491 SERHSQLGQPLAKKIGKLTELHQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEK 5549
Cdd:pfam05483  554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5437-5661 5.19e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5437 KIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELHQQtI 5516
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-L 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5517 RQAENRLSKLNQALSHMEEYNEMletvrkwiekaKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQH 5596
Cdd:COG4942    100 EAQKEELAELLRALYRLGRQPPL-----------ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907076625 5597 LANVycTGKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTS 5661
Cdd:COG4942    169 LEAE--RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
 
Name Accession Description Interval E-value
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
24-143 7.18e-71

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 233.81  E-value: 7.18e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21241     81 -------IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
182-290 1.49e-70

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 232.98  E-value: 1.49e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21243      1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                           90       100
                   ....*....|....*....|....*....
gi 1907076625  262 LLDPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21243     81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
24-143 6.31e-60

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 202.80  E-value: 6.31e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21190     81 -------IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
184-290 1.94e-54

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 186.86  E-value: 1.94e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21192      1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 1907076625  264 DPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21192     81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
24-143 2.27e-43

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 155.37  E-value: 2.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkrIHAVANIGTALKFLEGRK 103
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNV--FQCRSNIETALSFLKNKS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21242     79 -------IKLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
184-290 1.91e-42

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409094  Cd Length: 106  Bit Score: 152.25  E-value: 1.91e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKqMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21245      1 QRKAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLL 79
                           90       100
                   ....*....|....*....|....*..
gi 1907076625  264 DPEDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21245     80 EPEDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
182-289 3.06e-42

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 151.91  E-value: 3.06e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21244      1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
                           90       100
                   ....*....|....*....|....*...
gi 1907076625  262 LLDPEDVDVDKPDEKSIMTYVAQFLtQY 289
Cdd:cd21244     81 LLEPEDVDVVNPDEKSIMTYVAQFL-QY 107
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
186-290 1.25e-40

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 147.15  E-value: 1.25e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
28-141 1.54e-39

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 144.08  E-value: 1.54e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGRKsmyr 107
Cdd:cd21188      3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRK---- 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907076625  108 gspIKLVNINATDIADGRPSIVLGLMWTIILYFQ 141
Cdd:cd21188     75 ---IKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
28-142 8.37e-38

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 139.05  E-value: 8.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAK-RKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21186      2 VQKKTFTKWINSQLSKaNKPP--IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR--MRVHHLNNVNRALQVLEQNN--- 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21186     75 ----VKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
24-144 8.57e-37

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 136.56  E-value: 8.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEE 144
Cdd:cd21191     81 -------VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
187-285 1.43e-36

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 135.62  E-value: 1.43e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQH-TAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21194      3 AKDALLLWCQRkTAGYP-GVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASY 101
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
15-138 9.49e-36

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 133.58  E-value: 9.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   15 TNVMQRLQDEQEIVQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGT 94
Cdd:cd21193      3 KGRIRALQEERINIQKKTFTKWINSFL--EKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRL-RVQKIENVNK 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907076625   95 ALKFLEgrksmyrgSPIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21193     80 ALAFLK--------TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
187-285 2.02e-34

second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409097  Cd Length: 105  Bit Score: 129.44  E-value: 2.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQ-HTAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21248      3 AKDALLLWCQmKTAGYP-NVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTY 101
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
21-138 5.28e-34

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 128.64  E-value: 5.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   21 LQDEQEIVQKRTFTKWINSHLAKRkpPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALKFLE 100
Cdd:cd21246      9 LADEREAVQKKTFTKWVNSHLARV--GCRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKM-RIHCLENVDKALQFLK 85
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907076625  101 GRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21246     86 EQR-------VHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
15-145 1.70e-33

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 127.79  E-value: 1.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   15 TNVMQRLQDEQEIVQKRTFTKWINSHLAK-RKPpmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRvkRIHAVANIG 93
Cdd:cd21236      4 ENVLERYKDERDKVQKKTFTKWINQHLMKvRKH---VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQ 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907076625   94 TALKFLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEEL 145
Cdd:cd21236     79 IALDYLKRRQ-------VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
186-290 1.02e-31

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409088  Cd Length: 104  Bit Score: 121.63  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAEtQLGIPRLLDP 265
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
23-148 3.66e-30

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 117.82  E-value: 3.66e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   23 DEQEIVQKRTFTKWINSHLAKRKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGR 102
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907076625  103 KsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEELTSN 148
Cdd:cd21235     77 Q-------VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
189-290 9.08e-30

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409036  Cd Length: 104  Bit Score: 115.99  E-value: 9.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  189 KTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPEDV 268
Cdd:cd21187      3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
                           90       100
                   ....*....|....*....|..
gi 1907076625  269 DVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21187     83 NVEQPDKKSILMYVTSLFQVLP 104
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
24-283 1.19e-29

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 128.91  E-value: 1.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKPPMVvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRK 103
Cdd:COG5069      5 KWQKVQKKTFTKWTNEKLISGGQKEF-GDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  104 smyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEeltsnlpqlqslsssassvdsmvstetasppskrKVAAKI 183
Cdd:COG5069     84 -------VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIA----------------------------------TINEEG 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQH-TAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKV-KTRSNRE-NLEDAFTIAETQLGIP 260
Cdd:COG5069    123 ELTKHINLLLWCDEdTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIA 202
                          250       260
                   ....*....|....*....|....
gi 1907076625  261 RLLDPEDV-DVDKPDEKSIMTYVA 283
Cdd:COG5069    203 RLIGVEDIvNVSIPDERSIMTYVS 226
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
186-285 1.25e-29

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 116.26  E-value: 1.25e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21319      5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21319     85 EDVFTENPDEKSIITYVVAF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
186-285 1.36e-29

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 115.73  E-value: 1.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21249      4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21249     84 EDVAVPHPDERSIMTYVSLY 103
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
182-300 6.64e-29

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409170  Cd Length: 119  Bit Score: 114.38  E-value: 6.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  182 KIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPR 261
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907076625  262 LLDPEDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDGQ 300
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGK 119
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
186-290 1.20e-28

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409089  Cd Length: 107  Bit Score: 113.21  E-value: 1.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETqLGIPRLLDP 265
Cdd:cd21240      4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDA 82
                           90       100
                   ....*....|....*....|....*
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21240     83 EDVDVPSPDEKSVITYVSSIYDAFP 107
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
187-290 1.21e-28

second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409087  Cd Length: 106  Bit Score: 113.19  E-value: 1.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21238      3 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
                           90       100
                   ....*....|....*....|....
gi 1907076625  267 DVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21238     83 DVDVPQPDEKSIITYVSSLYDAMP 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
186-285 1.36e-28

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 113.23  E-value: 1.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21216     10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDA 89
                           90       100
                   ....*....|....*....|.
gi 1907076625  266 ED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21216     90 EDiVNTPRPDERSVMTYVSCY 110
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
23-143 1.39e-28

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 113.09  E-value: 1.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   23 DEQEIVQKRTFTKWINSHLAK-RKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEG 101
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGS--TRVHALNNVNKALQVLQK 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907076625  102 RKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21231     77 NN-------VDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
28-140 2.25e-28

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 112.11  E-value: 2.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKsmyr 107
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRG---- 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907076625  108 gspIKLVNINATDIADGRPSIVLGLMWTIILYF 140
Cdd:cd21215     78 ---VKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
18-138 6.28e-28

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 112.43  E-value: 6.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   18 MQRLQDEQEIVQKRTFTKWINSHLAkrKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALK 97
Cdd:cd21318     28 IKALADEREAVQKKTFTKWVNSHLA--RVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRM-RIHSLENVDKALQ 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907076625   98 FLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21318    105 FLKEQR-------VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
26-138 1.35e-27

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 110.17  E-value: 1.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   26 EIVQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPceQGHRVK-RIHAVANIGTALKFLEGRKs 104
Cdd:cd21214      3 EKQQRKTFTAWCNSHL--RKAGTQIENIEEDFRDGLKLMLLLEVISGERLP--KPERGKmRFHKIANVNKALDFIASKG- 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907076625  105 myrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21214     78 ------VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
23-145 2.13e-27

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 110.12  E-value: 2.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   23 DEQEIVQKRTFTKWINSHLAKRKPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRvkRIHAVANIGTALKFLEGR 102
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKH--INDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907076625  103 KsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIEEL 145
Cdd:cd21237     77 Q-------VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
187-285 2.34e-27

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 109.54  E-value: 2.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21291     11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90
                           90       100
                   ....*....|....*....|
gi 1907076625  267 DV-DVDKPDEKSIMTYVAQF 285
Cdd:cd21291     91 DVcDVAKPDERSIMTYVAYY 110
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
18-138 9.21e-27

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 108.60  E-value: 9.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   18 MQRLQDEQEIVQKRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALK 97
Cdd:cd21317     21 IKALADEREAVQKKTFTKWVNSHLARVT--CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRM-RIHCLENVDKALQ 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907076625   98 FLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21317     98 FLKEQK-------VHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
186-285 1.45e-25

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 104.41  E-value: 1.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTY 101
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
28-143 5.62e-25

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 102.78  E-value: 5.62e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKR-KPPmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHrvKRIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21232      2 VQKKTFTKWINARFSKSgKPP--IKDMFTDLRDGRKLLDLLEGLTGKSLPKERGS--TRVHALNNVNRVLQVLHQNN--- 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYFQIE 143
Cdd:cd21232     75 ----VELVNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
186-299 4.09e-24

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409171  Cd Length: 130  Bit Score: 100.90  E-value: 4.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21322     17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLDP 96
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQFLTQYPDIHGAGCDG 299
Cdd:cd21322     97 EDVNMEAPDEKSIITYVVSFYHYFSKMKALAVEG 130
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
26-142 6.55e-24

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 100.22  E-value: 6.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   26 EIVQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKSm 105
Cdd:cd21311     13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEDEG- 89
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907076625  106 yrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21311     90 -----IKIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
187-290 1.27e-23

second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 98.49  E-value: 1.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21234      1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
                           90       100
                   ....*....|....*....|....
gi 1907076625  267 DVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21234     81 DVAVQLPDKKSIIMYLTSLFEVLP 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
187-285 1.74e-23

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 98.19  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKW-VQHTAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21253      2 GIKALQQWcRQQTEGYR-DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                           90       100
                   ....*....|....*....|.
gi 1907076625  266 ED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21253     81 EDmVALKVPDKLSILTYVSQY 101
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
18-142 7.14e-23

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 97.14  E-value: 7.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   18 MQRLQDEQEIVQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPcEQGHRVKRIHAVANIGTALK 97
Cdd:cd21247     10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLP-RPSRGKMRVHFLENNSKAIT 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907076625   98 FLEGRksmyrgSPIKLvnINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21247     89 FLKTK------VPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
187-285 5.12e-22

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 94.14  E-value: 5.12e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21197      1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                           90       100
                   ....*....|....*....|
gi 1907076625  267 D-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21197     81 DmVTMHVPDRLSIITYVSQY 100
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
28-140 1.52e-21

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 92.93  E-value: 1.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVK-RIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21183      4 IQANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAfQQHYLENVSTALKFIEADH--- 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYF 140
Cdd:cd21183     79 ----IKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
187-285 2.29e-21

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 92.35  E-value: 2.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQ-HTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTR--SNRENLEDAFTIAETQLGIPR-L 262
Cdd:pfam00307    3 LEKELLRWINsHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|...
gi 1907076625  263 LDPEdvDVDKPDEKSIMTYVAQF 285
Cdd:pfam00307   83 IEPE--DLVEGDNKSVLTYLASL 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
28-142 9.94e-21

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 90.42  E-value: 9.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKsmyr 107
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTG--MSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDG---- 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907076625  108 gspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21227     78 ---IKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
18-138 1.04e-20

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 92.03  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   18 MQRLQDEQEIVQKRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVkRIHAVANIGTALK 97
Cdd:cd21316     43 IKALADEREAVQKKTFTKWVNSHLARVS--CRITDLYMDLRDGRMLIKLLEVLSGERLPKPTKGRM-RIHCLENVDKALQ 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907076625   98 FLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIIL 138
Cdd:cd21316    120 FLKEQR-------VHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
186-284 1.19e-20

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 90.18  E-value: 1.19e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAEtQLGIPRLLDP 265
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
                           90       100
                   ....*....|....*....|
gi 1907076625  266 ED-VDVDKPDEKSIMTYVAQ 284
Cdd:cd21198     80 ADmVLLSVPDKLSVMTYLHQ 99
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
184-285 1.79e-20

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 90.53  E-value: 1.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21290     11 ETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKML 90
                           90       100
                   ....*....|....*....|...
gi 1907076625  264 DPED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21290     91 DAEDiVNTARPDEKAIMTYVSSF 113
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
187-290 3.59e-20

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 89.22  E-value: 3.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKV-KTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21233      1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQHLGIEKLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQFLTQYP 290
Cdd:cd21233     81 EDVATAHPDKKSILMYVTSLFQVLP 105
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
189-285 5.71e-20

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 88.11  E-value: 5.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  189 KTLLKWVQ-HTAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd22198      3 EELLSWCQeQTEGYR-GVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81
                           90
                   ....*....|....*....
gi 1907076625  268 -VDVDKPDEKSIMTYVAQF 285
Cdd:cd22198     82 mASLAVPDKLSMVSYLSQF 100
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
187-285 8.95e-20

second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409033  Cd Length: 103  Bit Score: 87.68  E-value: 8.95e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGkqmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNR-ENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21184      2 GKSLLLEWVNSKIP---EYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEELGIPKIITP 78
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21184     79 EDMVSPNVDELSVMTYLSYF 98
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
187-285 1.73e-19

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 86.85  E-value: 1.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|
gi 1907076625  267 D-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQY 100
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
33-140 2.25e-19

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 86.48  E-value: 2.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   33 FTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKsmyrgspIK 112
Cdd:cd21212      5 YTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALG-------VD 77
                           90       100
                   ....*....|....*....|....*...
gi 1907076625  113 LVNINATDIADGRPSIVLGLMWTIILYF 140
Cdd:cd21212     78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
184-285 2.85e-19

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409136  Cd Length: 124  Bit Score: 87.06  E-value: 2.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21287      8 ETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKML 87
                           90       100
                   ....*....|....*....|...
gi 1907076625  264 DPED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21287     88 DAEDiVGTARPDEKAIMTYVSSF 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
28-142 1.15e-18

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 84.65  E-value: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPcEQGHRVKRIHAVANIGTALKFLEgrKSMyr 107
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-KKKLNKSEFDKLENINLALDVAE--KKL-- 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907076625  108 gsPIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:pfam00307   77 --GVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
184-285 1.77e-18

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 84.78  E-value: 1.77e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21289      8 ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKML 87
                           90       100
                   ....*....|....*....|...
gi 1907076625  264 DPED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21289     88 DAEDiVNTPKPDEKAIMTYVSCF 110
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
28-140 2.18e-18

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 83.69  E-value: 2.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHR-VKRIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21228      4 IQQNTFTRWCNEHL--KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYNKRpTFRQMKLENVSVALEFLERES--- 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYF 140
Cdd:cd21228     79 ----IKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
187-284 8.70e-18

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 82.14  E-value: 8.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAEtQLGIPRLLDPE 266
Cdd:cd21255      2 SSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEPA 80
                           90
                   ....*....|....*....
gi 1907076625  267 DVDVDK-PDEKSIMTYVAQ 284
Cdd:cd21255     81 DMVLLPiPDKLIVMTYLCQ 99
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
186-289 9.17e-18

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 82.21  E-value: 9.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  186 NAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAeTQLGIPRLLDP 265
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEP 79
                           90       100
                   ....*....|....*....|....*
gi 1907076625  266 ED-VDVDKPDEKSIMTYVAQFLTQY 289
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQIRAHF 104
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
189-285 2.41e-17

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 80.59  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  189 KTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPEDV 268
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90
                   ....*....|....*..
gi 1907076625  269 DVDKPDEKSIMTYVAQF 285
Cdd:cd21226     83 MTGNPDERSIVLYTSLF 99
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
188-282 1.46e-16

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 78.54  E-value: 1.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21200      3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVED 82
                           90
                   ....*....|....*..
gi 1907076625  268 VDV--DKPDEKSIMTYV 282
Cdd:cd21200     83 MVRmgNRPDWKCVFTYV 99
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
184-285 2.32e-16

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409137  Cd Length: 124  Bit Score: 78.58  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLL 263
Cdd:cd21288      8 ETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKML 87
                           90       100
                   ....*....|....*....|...
gi 1907076625  264 DPED-VDVDKPDEKSIMTYVAQF 285
Cdd:cd21288     88 DAEDiVNTPKPDERAIMTYVSCF 110
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
26-136 4.22e-16

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 77.57  E-value: 4.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   26 EIVQKRTFTKWINSHLAKRKPPMVvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVK-RIHAVANIGTALKFLEgrKS 104
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGIPKI-SDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKnRIQMIQNLHLAMLFIE--ED 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907076625  105 MyrgsPIKLVNINATDIADGRPSIVLGLMWTI 136
Cdd:cd21225     79 L----KIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
179-284 5.03e-16

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 77.40  E-value: 5.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  179 VAAKIQGNAKKTLLKWVQH-TAGKQmGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQl 257
Cdd:cd21199      1 LARRYGGSKRNALLKWCQEkTQGYK-GIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV- 78
                           90       100
                   ....*....|....*....|....*...
gi 1907076625  258 GIPRLLDPED-VDVDKPDEKSIMTYVAQ 284
Cdd:cd21199     79 GIPTTLTIDEmVSMERPDWQSVMSYVTA 106
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
191-291 1.93e-15

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 75.46  E-value: 1.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  191 LLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLD-PEDVD 269
Cdd:cd21195      9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
                           90       100
                   ....*....|....*....|..
gi 1907076625  270 VDKPDEKSIMTYVAQFLTQYPD 291
Cdd:cd21195     89 AQEPDKLSMVMYLSKFYELFRG 110
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
189-285 5.27e-15

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 73.89  E-value: 5.27e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   189 KTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNR----ENLEDAFTIAETQLGIPRLLD 264
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1907076625   265 PEDVDVDKPDEKSIMTYVAQF 285
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
188-285 5.54e-15

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 74.26  E-value: 5.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21259      3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
                           90
                   ....*....|....*....
gi 1907076625  268 -VDVDKPDEKSIMTYVAQF 285
Cdd:cd21259     83 mVRMREPDWKCVYTYIQEF 101
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
28-142 1.03e-14

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 73.91  E-value: 1.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLAKRKPPMvvDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVK-RIHAVANIGTALKFLEGRKsmy 106
Cdd:cd21310     16 IQQNTFTRWCNEHLKCVQKRL--NDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNfRQMKLENVSVALEFLDREH--- 90
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21310     91 ----IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
187-285 1.78e-14

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409079  Cd Length: 103  Bit Score: 72.42  E-value: 1.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  187 AKKTLLKWVQHtagKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRLLDP 265
Cdd:cd21230      2 PKQRLLGWIQN---KIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLITP 78
                           90       100
                   ....*....|....*....|
gi 1907076625  266 EDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21230     79 EEIINPNVDEMSVMTYLSQF 98
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
30-138 1.95e-14

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 72.37  E-value: 1.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   30 KRTFTKWINSHLAKRKPPmVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKSMyrgs 109
Cdd:cd00014      1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLP---- 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907076625  110 piKLVNINATDI-ADGRPSIVLGLMWTIIL 138
Cdd:cd00014     76 --ELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
191-291 8.35e-14

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 70.75  E-value: 8.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  191 LLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGI-PRLLDPEDVD 269
Cdd:cd21251     10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGIsPIMTGKEMAS 89
                           90       100
                   ....*....|....*....|..
gi 1907076625  270 VDKPDEKSIMTYVAQFLTQYPD 291
Cdd:cd21251     90 VGEPDKLSMVMYLTQFYEMFKD 111
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
31-139 1.64e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 69.65  E-value: 1.64e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625    31 RTFTKWINSHLAKRKPPmVVDDLFEDMKDGIKLLALLEVLSGQKLPceqgHRVK-----RIHAVANIGTALKFLEGRKsm 105
Cdd:smart00033    1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVD----KKKVaaslsRFKKIENINLALSFAEKLG-- 73
                            90       100       110
                    ....*....|....*....|....*....|....
gi 1907076625   106 yrgspIKLVNINATDIADGRPSIvLGLMWTIILY 139
Cdd:smart00033   74 -----GKVVLFEPEDLVEGPKLI-LGVIWTLISL 101
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
179-284 4.11e-13

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 68.90  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  179 VAAKIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETqLG 258
Cdd:cd21257      1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VG 79
                           90       100
                   ....*....|....*....|....*..
gi 1907076625  259 I-PRLLDPEDVDVDKPDEKSIMTYVAQ 284
Cdd:cd21257     80 IkPSLELSEMMYTDRPDWQSVMQYVAQ 106
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
188-285 7.77e-13

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 68.19  E-value: 7.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90
                   ....*....|....*....
gi 1907076625  268 -VDVDKPDEKSIMTYVAQF 285
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQEL 101
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
188-282 1.14e-12

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 67.68  E-value: 1.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21261      3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
                           90
                   ....*....|....*..
gi 1907076625  268 VDV--DKPDEKSIMTYV 282
Cdd:cd21261     83 MMVmgRKPDPMCVFTYV 99
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
28-142 1.77e-12

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 67.80  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLA---KRkppmvVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVK-RIHAVANIGTALKFLEgRK 103
Cdd:cd21308     20 IQQNTFTRWCNEHLKcvsKR-----IANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTfRQMQLENVSVALEFLD-RE 93
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907076625  104 SmyrgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21308     94 S------IKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
28-142 2.54e-12

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 67.41  E-value: 2.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   28 VQKRTFTKWINSHLakRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVK-RIHAVANIGTALKFLEgRKSmy 106
Cdd:cd21309     17 IQQNTFTRWCNEHL--KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRPTfRQMQLENVSVALEFLD-RES-- 91
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907076625  107 rgspIKLVNINATDIADGRPSIVLGLMWTIILYFQI 142
Cdd:cd21309     92 ----IKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
188-288 3.63e-12

second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409078  Cd Length: 105  Bit Score: 65.87  E-value: 3.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQhTAGKQMGIevKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21229      5 KKLMLAWLQ-AVLPELKI--TNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90       100
                   ....*....|....*....|..
gi 1907076625  267 DVDVDKPDEKSIMTYVAQFLTQ 288
Cdd:cd21229     82 DLSSPHLDELSGMTYLSYFMKE 103
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
30-137 3.72e-12

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 66.06  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   30 KRTFTKWINSHLA-----KRKPPMV--VDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRI---HAVANIGtalKFL 99
Cdd:cd21217      3 KEAFVEHINSLLAddpdlKHLLPIDpdGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKKPKnifEATENLN---LAL 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907076625  100 EGRKSMyrGspIKLVNINATDIADGRPSIVLGLMWTII 137
Cdd:cd21217     80 NAAKKI--G--CKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
188-285 4.83e-12

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 65.96  E-value: 4.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQhtaGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21315     18 KQRLLGWIQ---SKVPDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPE 94
                           90
                   ....*....|....*....
gi 1907076625  267 DVDVDKPDEKSIMTYVAQF 285
Cdd:cd21315     95 EMVNPKVDELSMMTYLSQF 113
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
191-285 5.61e-12

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 65.67  E-value: 5.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  191 LLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLD-PEDVD 269
Cdd:cd21250      9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                           90
                   ....*....|....*.
gi 1907076625  270 VDKPDEKSIMTYVAQF 285
Cdd:cd21250     89 AEEPDKLSMVMYLSKF 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
188-282 7.73e-12

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409107  Cd Length: 111  Bit Score: 65.45  E-value: 7.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21258      3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                           90
                   ....*....|....*..
gi 1907076625  268 VDV--DKPDEKSIMTYV 282
Cdd:cd21258     83 MMImgKKPDSKCVFTYV 99
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
179-282 1.15e-11

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 65.09  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  179 VAAKIQGNAKKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETqLG 258
Cdd:cd21256      7 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VG 85
                           90       100
                   ....*....|....*....|....*
gi 1907076625  259 IPRLLDPED-VDVDKPDEKSIMTYV 282
Cdd:cd21256     86 IKSTLDINEmVRTERPDWQSVMTYV 110
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
188-285 1.70e-11

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 63.90  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSN---RENLEDAFTIAETQ-LGIPRLL 263
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
                           90       100
                   ....*....|....*....|..
gi 1907076625  264 DPEDVdVDKPDEKSIMTYVAQF 285
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWAL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4967-5802 6.00e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.70  E-value: 6.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4967 LEHTLAELQELDgDVQEALRTRQATLTEIYSRCQRYYQvfqaandwLDDAQEMLQLAGNGLDVESAEENLRshmEFFKTE 5046
Cdd:TIGR02168  181 LERTRENLDRLE-DILNELERQLKSLERQAEKAERYKE--------LKAELRELELALLVLRLEELREELE---ELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5047 GQFHSNMEELRGLVARLDPLIkatgkEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVielmNDAEK 5126
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKL-----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL----ERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5127 KLSEFAVLKTSSIHEAEEKLskhKALVSVVDSFHEKIVALEEKASQLEQTgndtsKATLSRSMTTVWQRWTRLR-AVAQD 5205
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEELEAE-----LEELESRLEELEEQLETLRsKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5206 QEKI------LEDAVDEWKRLSAKVKETTEVINQLQGRLpgsstEKASKAELMTLLESHDTYLMDLESQQLTLgvlqQRA 5279
Cdd:TIGR02168  392 ELQIaslnneIERLEARLERLEDRRERLQQEIEELLKKL-----EEAELKELQAELEELEEELEELQEELERL----EEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5280 LSMLQDRAFPGTEEEVPI---LRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYlgnpTIE 5356
Cdd:TIGR02168  463 LEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY----EAA 538
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5357 IDTQLEElkRLLAEATSHQESIEKIAEEQKNKYLGLYTVLP-------------SEISLQLAEVALDLKIHDQIQEK--- 5420
Cdd:TIGR02168  539 IEAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndREILKNIEGFLGVAKDLVKFDPKlrk 616
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5421 -----------VQEIEEGKAMSQEFSCKIQKVTKDLTTI-----LTKLKAKTDD-LVHAKAEHKMLGEELDGCNSKLMEL 5483
Cdd:TIGR02168  617 alsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvITGGSAKTNSsILERRREIEELEEKIEELEEKIAEL 696
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5484 DAAIQTFSERHSQLGQPLAKKIGKLTEL-------------HQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKA 5550
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELsrqisalrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5551 KVLVHGNIAwnsasQLQEQYilhQTLLEESGEIDSDLEAMAEKVQHLANVYctGKLSQQVTQFGREMEELRQAIRVRLRN 5630
Cdd:TIGR02168  777 LAEAEAEIE-----ELEAQI---EQLKEELKALREALDELRAELTLLNEEA--ANLRERLESLERRIAATERRLEDLEEQ 846
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5631 LQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLchrQHLLSEMESLKPKMQAVQLCQSALRipedvvasl 5710
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL---ALLRSELEELSEELRELESKRSELR--------- 914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5711 plcHAALRLQEEASQLQhtaiqqcnimqeavVQYEQYKQEMKHLQQLIEEAHREIEDKPVATSNIQELQAqislhEELAQ 5790
Cdd:TIGR02168  915 ---RELEELREKLAQLE--------------LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE-----EEARR 972
                          890
                   ....*....|..
gi 1907076625 5791 KIKGYQEQIDSL 5802
Cdd:TIGR02168  973 RLKRLENKIKEL 984
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
49-137 1.46e-10

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 61.84  E-value: 1.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   49 VVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGH-----RVKRIHavaNIGTALKFLEGRKSMYRGSpikLVNINATDIAD 123
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRvpaisRLQKLH---NVEVALKALKEAGVLRGGD---GGGITAKDIVD 98
                           90
                   ....*....|....
gi 1907076625  124 GRPSIVLGLMWTII 137
Cdd:cd21223     99 GHREKTLALLWRII 112
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5000-5213 2.91e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 63.62  E-value: 2.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5000 QRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTEGQFHSNMEELRGLVARLDPLiKATGKEELAQKM 5079
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5080 ASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREgVIELMNDAEKKLSefAVLKTSSIHEAEEKLSKHKALVSVVDSF 5159
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907076625 5160 HEKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQEKILEDA 5213
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3821-4011 3.11e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 63.62  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3821 LAKEFSDKYKVLAQWMAEyQEILCTPEEPKMELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQS--LKD 3898
Cdd:cd00176      1 KLQQFLRDADELEAWLSE-KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3899 KIQKLQSDFQDLCSRAKERVFSLEAKVKDHEdYNTELQEVEKWLLQMSGRLVAPDLLEmsSLETITQQLAHHKAMMEEIA 3978
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELE 156
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907076625 3979 GFEDRLDNLKAKGDTLIGQCPEHLQAKQKQTVQ 4011
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
184-285 3.67e-10

second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409163  Cd Length: 115  Bit Score: 60.47  E-value: 3.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  184 QGNAKKTLLKWVQHTAGKqmgIEVKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRL 262
Cdd:cd21314      9 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
                           90       100
                   ....*....|....*....|...
gi 1907076625  263 LDPEDVDVDKPDEKSIMTYVAQF 285
Cdd:cd21314     86 IAPEEIVDPNVDEHSVMTYLSQF 108
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
188-285 8.88e-10

second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409162  Cd Length: 110  Bit Score: 59.34  E-value: 8.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHtagKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21313     10 KQRLLGWIQN---KIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVITPE 86
                           90
                   ....*....|....*....
gi 1907076625  267 DVDVDKPDEKSIMTYVAQF 285
Cdd:cd21313     87 EIIHPDVDEHSVMTYLSQF 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
29-124 2.08e-09

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 58.08  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   29 QKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLP-------CEQGHRvkrihavANIGTALKFLEG 101
Cdd:cd21213      1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgidwnptTDAERK-------ENVEKVLQFMAS 73
                           90       100
                   ....*....|....*....|...
gi 1907076625  102 RKsmyrgspIKLVNINATDIADG 124
Cdd:cd21213     74 KR-------IRMHQTSAKDIVDG 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1167-2008 3.59e-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: 63.92  E-value: 3.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1167 DEVKHMVDEIRNDITKKGESLSWLKSRLkylidisseneaQKRGDELAELSSSFKALVALLSEVEkllsnfgecvQYKEI 1246
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEV------------SELEEEIEELQKELYALANEISRLE----------QQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1247 VKSSLEGLisgpQESKEEAEMILDsknllEAQQLLLHHQQKTKMISAKKRDLQEQMEQAQQGGQAGPgqEELRKLESTLT 1326
Cdd:TIGR02168  307 LRERLANL----ERQLEELEAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELE--AELEELESRLE 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1327 GLEQSRERQERRIqVSLRkwERFETNKETVVRYLFQTGSSHERFLSFSSLESLSSELEQTKEFSKRTESIATQAENLVKE 1406
Cdd:TIGR02168  376 ELEEQLETLRSKV-AQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1407 AAELPLGPRNKRVLQRQAKSIKEQVTTLEDTLEEDIKTMEMVKSKWDHFGSNFETLSIWILEKEnelssleASASAADVQ 1486
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS-------GLSGILGVL 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1487 ISQIKVTiQEIESKIDsiVGLEEEAQSFaqfVTTGESARIKAkltqirryWEELQEHARGLEGTILGHLSQQQKFEENLR 1566
Cdd:TIGR02168  526 SELISVD-EGYEAAIE--AALGGRLQAV---VVENLNAAKKA--------IAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1567 KIRQSVSEFAERLADPIKIcssAAETYKVLQEHMDLCQAVESLSST-------------VT-----------MFSASAQK 1622
Cdd:TIGR02168  592 EILKNIEGFLGVAKDLVKF---DPKLRKALSYLLGGVLVVDDLDNAlelakklrpgyriVTldgdlvrpggvITGGSAKT 668
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1623 AVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQL 1702
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1703 IQALQNEVVSQASLYSNLLQLKEALFS--VASKEDVAVMKLQLEQLDERWGDLPQIISkrmhflqsvlAEHKQFDELlfs 1780
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALD----------ELRAELTLL--- 815
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1781 fsvwiKQFLGELQRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAqdlhpLQSKVDDCFQLFEEA 1860
Cdd:TIGR02168  816 -----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-----LESELEALLNERASL 885
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1861 SQVVERRKLALAQLAEFLQSHACMSTLLYQLRQtvEATKSMSKkqsdsLKTDLHSAIQDVKTLESSAISLDGTLTKAQCH 1940
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 1941 LKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEE---RMDRE 2008
Cdd:TIGR02168  959 LENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEaieEIDRE 1029
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4896-5686 6.93e-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: 63.15  E-value: 6.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4896 EMSRSLDWLRR--VKAElsgpvcldlSLQDIQEEIRKIQIHqeevLSSLRIMSALSHKEQekftkakelisadLEHTLAE 4973
Cdd:TIGR02168  197 ELERQLKSLERqaEKAE---------RYKELKAELRELELA----LLVLRLEELREELEE-------------LQEELKE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4974 LQELDGDVQEALRTRQATLTEIYSRcqryyqvFQAANDWLDDAQEMLQLAGNglDVESAEENLRSHMEffktegQFHSNM 5053
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALAN--EISRLEQQKQILRE------RLANLE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5054 EELRGLVARLDPLIKAtgKEELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKAREGVIELMNDAEKKlsefav 5133
Cdd:TIGR02168  316 RQLEELEAQLEELESK--LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK------ 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5134 lktssIHEAEEKLSKHKALVSVVDSfheKIVALEEKASQLEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQEKILEDA 5213
Cdd:TIGR02168  388 -----VAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5214 VDEWKRLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLLESHDTYLMDLESQQLTLGVLQQRALSMLQDRAfpgtEE 5293
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE----GY 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5294 EVPILRAITA-LQDQCLNMQEKVKNHGKLVKQELQEREAV-------ETRINSVKSWVQETKDYLGNPTIEIDTQLEELK 5365
Cdd:TIGR02168  536 EAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFlpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5366 RLLAEATSHQESIEKIAE--EQKNKYLGLYTVLPSEISLQLAEVAL---DLKIHDQIQEKVQEIEEGKAMSQEFSCKIQK 5440
Cdd:TIGR02168  616 KALSYLLGGVLVVDDLDNalELAKKLRPGYRIVTLDGDLVRPGGVItggSAKTNSSILERRREIEELEEKIEELEEKIAE 695
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5441 VTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELH-------- 5512
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerleeaee 775
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5513 ------------QQTIRQAENRLSKLNQALSHME-EYNEMLETVRKWIEKAKVLVHgniawNSASQLQEQYILHQTLLEE 5579
Cdd:TIGR02168  776 elaeaeaeieelEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLER-----RIAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5580 SGEIDSDLEAMAEKVQHLAnvyctgKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTIL 5659
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIE------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          810       820
                   ....*....|....*....|....*..
gi 1907076625 5660 TSPEVGRRSLKEQLCHRQHLLSEMESL 5686
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERLSEEYSL 951
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4595-5396 1.90e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4595 LMNEKTELHAQLDKYQSILEqspEYENLLLTLQTTGQAMLPSLNEVD--HSYLSEKLSALPQQFNVIVALAKDKfykTQE 4672
Cdd:TIGR02168  230 LVLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRL---EQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4673 AILARKEYTSLieltTQSLGDLEDQFLKMRKMPSDLIvEESVSLQQSCSALLGEVVALGEAVNELNQKKESFRSTGQPWQ 4752
Cdd:TIGR02168  304 KQILRERLANL----ERQLEELEAQLEELESKLDELA-EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4753 pEKMLQLATLYHRLKRQAEQrvsfLEDTTSVYKEHAQmcrQLESQLEVVKREQAKVNEETLPAEEKLkvyhsLAGSLQDS 4832
Cdd:TIGR02168  379 -EQLETLRSKVAQLELQIAS----LNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEEL 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4833 GILLKRVATHLEDLSphldpTAYEKAKSQVQSWQEELKQMTSDVGELVTECESRMVQSIDFQTEmSRSLDWLRRVKAELS 4912
Cdd:TIGR02168  446 EEELEELQEELERLE-----EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-SEGVKALLKNQSGLS 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4913 GPVCLDLSLQDIQEEIRKIQihqEEVLSSlRIMSALShkeqEKFTKAKELISADLEH-----TLAELQELDGDVQEALRT 4987
Cdd:TIGR02168  520 GILGVLSELISVDEGYEAAI---EAALGG-RLQAVVV----ENLNAAKKAIAFLKQNelgrvTFLPLDSIKGTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4988 RQATLTEiysrcqryyqVFQAANDWLDDAQEMLQLAGNGL--------DVESAEE---NLRSHMEFFKTEGQF------- 5049
Cdd:TIGR02168  592 EILKNIE----------GFLGVAKDLVKFDPKLRKALSYLlggvlvvdDLDNALElakKLRPGYRIVTLDGDLvrpggvi 661
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5050 --------------HSNMEELRGLVARLDPLIKATGKE--ELAQKMASLEKRSQGIIQESHTQRDLLQRCMVQWQEYQKA 5113
Cdd:TIGR02168  662 tggsaktnssilerRREIEELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5114 REGVIELMNDAEKKLSEFAVLKTSSIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDTSKA--TLSRSMTT 5191
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltLLNEEAAN 821
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5192 VWQRWTRLRAVAQDQEKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTE-------KASKAELMTLLEShdtylmD 5264
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRS------E 895
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5265 LESQQLTLGVLQQRALSMLQDRAfPGTEEEVPILRAITALQDQCLNMQEKVKNHGKLVKQELQ--------EREAVETRI 5336
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELE-ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEalenkiedDEEEARRRL 974
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 5337 NSVKswvqETKDYLGNPTIEIDTQLEELK-RL---------LAEA-TSHQESIEKIAEEQKNKYLGLYTVL 5396
Cdd:TIGR02168  975 KRLE----NKIKELGPVNLAAIEEYEELKeRYdfltaqkedLTEAkETLEEAIEEIDREARERFKDTFDQV 1041
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
188-289 2.32e-08

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 55.05  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHTAGKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPED 267
Cdd:cd21196      5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
                           90       100
                   ....*....|....*....|..
gi 1907076625  268 VdVDKPDEKSIMTYVAQFLTQY 289
Cdd:cd21196     85 V-VAGSDPLGLIAYLSHFHSAF 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3394-3599 3.90e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 57.46  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3394 KWTSYQDDVRQFSSWMDSVEVSL--TESEKQHTELREKITalgKAKLLNEEVLSHSSLLETIEVKRAAMTEHY-----VT 3466
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLssTDYGDDLESVEALLK---KHEALEAELAAHEERVEALNELGEQLIEEGhpdaeEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3467 QLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYqRDLKAFESWLEQEQEKLDRcSVHEGDTNAHETMLRDLQELQVRC 3546
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907076625 3547 AEGQALLNSVLHTREDVIPSGLPQAEDRV---LESLRQDWQVYQHRLAEARMQLNN 3599
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEE 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3091-3661 7.08e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 7.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3091 TAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLNTMLFKGELlSSLLTEEKAQAVQAKVLTAKEEWKSFHANLHQKES 3170
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEA 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3171 ALENLKIQMKDFEVSAELVQNWLSKTERLVQESSNRLYDLPAK----RREQQKLQSVLEEiQCYEPQLHRLKEKARQLWE 3246
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEE-LLKKLEEAELKELQAELEE 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3247 GQAASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRIIAEHNRFSQGVKELQDWMSDAVHMLDSYCLPTSDKSVLDSRMLK 3326
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3327 LEALLSVRQEKEIQMkmvvtrgEYVLQSTSLegsAAVQQQLQAVKDMWESLLSAAIRCKSQLEGALSKWTSYQDDVRQFS 3406
Cdd:TIGR02168  525 LSELISVDEGYEAAI-------EAALGGRLQ---AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3407 SWMDSVEVSLTESEKQHTELREKI--------------TALGKAKLLNEE---------------------------VLS 3445
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILE 674
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3446 HSSLLETIEVKRAAMTEHY-VTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRCSV 3524
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3525 HEGDTNAHETMLRD----LQELQVRCAEGQALLNSVLHTREDVIpsglpQAEDRVLESLRQDWQVYQHRLAEARMQLNNV 3600
Cdd:TIGR02168  755 ELTELEAEIEELEErleeAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAANLRERLESL 829
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 3601 VNKLRLMEQKFQQADEWLKRMEEKInfrSECQSSRSDKEIQLLQLKKWHEDLSAHRDEVEE 3661
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERASLEE 887
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3927-4153 1.03e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 56.30  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3927 DHEDYNTELQEVEKWLLQMSGRLVAPDLLemSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHlqakq 4006
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD----- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4007 KQTVQAHLQGTKDSYSAICSTAQRVYRSLEYELQKHVSSQDtLQQCQAWISAVQPDLKpSPQPPLSRAEAVKQVKHFRAL 4086
Cdd:cd00176     74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKEL 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4087 QEQARTYLDLLCSMCDLSNSSVKNtakdiqQTEQLIEQRLVQAQNLTQGWEEIKSLKAELWIYLQDA 4153
Cdd:cd00176    152 EEELEAHEPRLKSLNELAEELLEE------GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
188-285 1.44e-07

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409161  Cd Length: 114  Bit Score: 53.27  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  188 KKTLLKWVQHtagKQMGIEVKDFGKSWRTGLAFHSVIHAIQPELV-DLEKVKTRSNRENLEDAFTIAETQLGIPRLLDPE 266
Cdd:cd21312     14 KQRLLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPE 90
                           90
                   ....*....|....*....
gi 1907076625  267 DVDVDKPDEKSIMTYVAQF 285
Cdd:cd21312     91 EIVDPNVDEHSVMTYLSQF 109
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
29-143 1.55e-07

first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409141  Cd Length: 145  Bit Score: 53.82  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   29 QKRTFTKWINSHLA-----KRKPPMVV--DDLFEDMKDGIKLLALLEV----------LSGQKLpceqghRVKRIHAvaN 91
Cdd:cd21292     25 EKVAFVNWINKNLGddpdcKHLLPMDPntDDLFEKVKDGILLCKMINLsvpdtideraINKKKL------TVFTIHE--N 96
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625   92 IGTALkflegrksmYRGSPI--KLVNINATDIADGRPSIVLGLMWTII---LYFQIE 143
Cdd:cd21292     97 LTLAL---------NSASAIgcNVVNIGAEDLKEGKPHLVLGLLWQIIrigLFADIE 144
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3181-3392 1.82e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 55.53  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3181 DFEVSAELVQNWLSKTERLVQeSSNRLYDLPAKRREQQKLQSVLEEIQCYEPQLHRLKEKARQLWEGQAASKSFVH-RVS 3259
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQeRLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3260 QLSSQYLALSNVTKEKVSRLDRIIAEHnRFSQGVKELQDWMSDAVHMLDSYcLPTSDKSVLDSRMLKLEALLSVRQEKEI 3339
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 3340 QMKMVVTRGEYVLQSTSLEGSAAVQQQLQAVKDMWESLLSAAIRCKSQLEGAL 3392
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2281-3120 2.44e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 2.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2281 IEADLRQKLEHAKEITEEARGTLKdFTAQRtqverfvkditawlinvEESLTRCAQTEtcEGLKKAKDIRKELQSQQNSI 2360
Cdd:TIGR02168  146 ISEIIEAKPEERRAIFEEAAGISK-YKERR-----------------KETERKLERTR--ENLDRLEDILNELERQLKSL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2361 TST----------QEELNSLCRKHHSVELESLGRAMTGLIKKHEATSQLCSQTQARIQDSLEKH-----FSGSMKEFQEW 2425
Cdd:TIGR02168  206 ERQaekaerykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlEVSELEEEIEE 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2426 FLGA-KAAARESSNLTGDSQILEARLHNLQGVLDSLSD----GQSKLDVVtqegqtlyahlpKQIVSSIQEQITKANEEF 2500
Cdd:TIGR02168  286 LQKElYALANEISRLEQQKQILRERLANLERQLEELEAqleeLESKLDEL------------AEELAELEEKLEELKEEL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2501 QAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTEN--LGESKHHISEKKNEVRKVEMFLGELLAARESL 2578
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2579 DKLSQRGQL--LSEESHSAGKGGCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSMWARVKDVQDRLACAes 2656
Cdd:TIGR02168  434 ELKELQAELeeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL-- 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2657 tLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLE---------MLKKAWAEAMNSAVH 2727
Cdd:TIGR02168  512 -LKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKqnelgrvtfLPLDSIKGTEIQGND 590
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2728 AQS--TLESVIDQWNDYLEKKSQLEQWMES------VDQRLEHPLQLQPGLKEKFSL--LDHFQ-----SIVSEAEDHTG 2792
Cdd:TIGR02168  591 REIlkNIEGFLGVAKDLVKFDPKLRKALSYllggvlVVDDLDNALELAKKLRPGYRIvtLDGDLvrpggVITGGSAKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2793 ALQQLAAKSRELYQK----TQDESFKEAGQEELRTQFQDIMTVAKEKMRTVEDLVKD-HLMYLDavqefadwLHSAKEEL 2867
Cdd:TIGR02168  671 SILERRREIEELEEKieelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKD--------LARLEAEV 742
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2868 HRWSDTSGDPSATQKKLLKIKELIDSREIGA-GRLSRVESLAPAVKQ--NTAASGCELLNSEMQALRADWRQWEDCLFQT 2944
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAeEELAEAEAEIEELEAqiEQLKEELKALREALDELRAELTLLNEEAANL 822
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2945 QSSLESLVSEMALSEQEFfgqvTQLEQALEQFctllktwAQQLTLLEGknsdeEILECWHKGREILDALQKA----EPMT 3020
Cdd:TIGR02168  823 RERLESLERRIAATERRL----EDLEEQIEEL-------SEDIESLAA-----EIEELEELIEELESELEALlnerASLE 886
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3021 EDLKSQLNELCRFSRDLSPYSEKVSGLIKEYNCLCLQASKGCQNKEQILQERFQKASRGFQQWLVNAKittakcfDLPQN 3100
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE-------EAEAL 959
                          890       900
                   ....*....|....*....|
gi 1907076625 3101 LSEVSSSLQKIQEFLSESEN 3120
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLEN 979
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
23-139 5.45e-07

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 51.51  E-value: 5.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   23 DEQEivqKRTFTKWINSHLakrkPPMVVDDLFEDMKDGIKLLALLEVLSGqklPCEQGHRVKR------IHAVANIGTAL 96
Cdd:cd21219      2 GSRE---ERAFRMWLNSLG----LDPLINNLYEDLRDGLVLLQVLDKIQP---GCVNWKKVNKpkplnkFKKVENCNYAV 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907076625   97 KFLEGRKsmyrgspIKLVNINATDIADGRPSIVLGLMWTIILY 139
Cdd:cd21219     72 DLAKKLG-------FSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1660-1873 2.37e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1660 RWQRLEKGLSPFLTWLERCEAIASSPekDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALfSVASKEDVAVM 1739
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1740 KLQLEQLDERWGDLPQIISKRMHFLQSVLAEHKQFDELLfSFSVWIKQFLGELQRTSEI-NLRDHQVALTRHKDHAAEIE 1818
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907076625 1819 KKRGEITHLQGHLSQLRSLGRAQDLHPLQSKVDDCFQLFEEASQVVERRKLALAQ 1873
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4349-4565 2.63e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 52.06  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4349 ELNVIQSRFQELMEWAEEQQpNIVEALKQSPPPGMAQHLLMDHLAICSELEAKQVLLKSLMKDADRvMADLGLNERKVIQ 4428
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4429 KALSEAQKHVSCLSDLVGQRRKYLNKALsEKTQFLMAVFQATSQIQQHERKIVfREYICLLPDDVSKQVKTCKTAQASLK 4508
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 4509 TYQNEVTGLCAQGRELMKGITKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSL 4565
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1494-2078 3.08e-06

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: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1494 IQEIESKIDSivgLEEEAQSFAQFVTTGESARIK------AKLTQIRRYWEELQEHARGLEGTILGHLSQQQKFEENLRK 1567
Cdd:COG1196    195 LGELERQLEP---LERQAEKAERYRELKEELKELeaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1568 IRQSVSEFAERLADpikicsSAAETYKVLQEHMDLCQAVESLSSTVTMFSASAQKAVNR--------ESCTQEAAALQQQ 1639
Cdd:COG1196    272 LRLELEELELELEE------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleeelEELEEELEELEEE 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1640 YEEILHKAKEMQTALEDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQLIQALQNEvvsQASLYSN 1719
Cdd:COG1196    346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEE 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1720 LLQLKEALFSVASKEDVAVMKLQLEQLDERwgdlpQIISKRMHFLQSVLAEHKQFDELLfsfSVWIKQFLGELQRTSEIN 1799
Cdd:COG1196    423 LEELEEALAELEEEEEEEEEALEEAAEEEA-----ELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLL 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1800 LRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGRAQDLHP-------LQSKVDDcfqLFEEASQVVERRKLALA 1872
Cdd:COG1196    495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaaLQNIVVE---DDEVAAAAIEYLKAAKA 571
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1873 QLAEFLQSHAcMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESSAISLDGTLTKAQCHLKSASPEERTSC 1952
Cdd:COG1196    572 GRATFLPLDK-IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1953 RATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMDRERLKVPTRQALQHRLRVFNQLEDEL 2032
Cdd:COG1196    651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 1907076625 2033 NSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRRQI 2078
Cdd:COG1196    731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
31-139 4.58e-06

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 48.49  E-value: 4.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   31 RTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKSMYRGsp 110
Cdd:cd21286      3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG-- 80
                           90       100
                   ....*....|....*....|....*....
gi 1907076625  111 iklvnINATDIADGRPSIVLGLMWTIILY 139
Cdd:cd21286     81 -----LSAEEIRNGNLKAILGLFFSLSRY 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1596-1768 4.63e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 51.29  E-value: 4.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1596 LQEHMDLCQAVESLSSTVTMFSASAQKAVNRESC-----TQEAAALQQQYEEILHKAKEMQTALEDLLARWQRLEKGLSp 1670
Cdd:cd00176     39 LKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaeeiQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD- 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1671 FLTWLERCEAIASSPekDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALFSVASKEDVAVMKLQLEQLDERW 1750
Cdd:cd00176    118 LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERW 195
                          170
                   ....*....|....*...
gi 1907076625 1751 GDLPQIISKRMHFLQSVL 1768
Cdd:cd00176    196 EELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5106-5328 4.81e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 51.29  E-value: 4.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5106 QWQEYQKAREGVIELMNDAEKKLSEFAVLKtsSIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDtSKATL 5185
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5186 SRSMTTVWQRWTRLRAVAQDQEKILEDAVDEWKRLSaKVKETTEVINQLQGRLPGSSTEKaSKAELMTLLESHDTYLMDL 5265
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 5266 ESQQLTLGVLQQRALSMLQDRAFPGTEEevpilraITALQDQCLNMQEKVKNHGKLVKQELQE 5328
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEE-------IEEKLEELNERWEELLELAEERQKKLEE 211
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
29-139 5.43e-06

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409148  Cd Length: 114  Bit Score: 48.65  E-value: 5.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   29 QKRTFTKWINSHLAKrkppMVVDDLFEDMKDGIKLLALLEVLS--------GQKLPCEQGHR-VKRIHAVANIGTALKFl 99
Cdd:cd21299      5 EERCFRLWINSLGID----TYVNNVFEDVRDGWVLLEVLDKVSpgsvnwkhANKPPIKMPFKkVENCNQVVKIGKQLKF- 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907076625  100 egrksmyrgspiKLVNINATDIADGRPSIVLGLMWTIILY 139
Cdd:cd21299     80 ------------SLVNVAGNDIVQGNKKLILALLWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2414-2619 5.90e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2414 HFSGSMKEFQEWfLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQSKLDVVTQEGQTLYAHLPKQIvSSIQEQI 2493
Cdd:cd00176      4 QFLRDADELEAW-LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2494 TKANEEFQAFLKQCLKEKQALQDCVSELGSFEDqHRKLNLWIHEMEERLKTENLGESKHHISEKkneVRKVEMFLGELLA 2573
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEEL---LKKHKELEEELEA 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907076625 2574 ARESLDKLSQRGQLLSEESHSAGKGGCRST--QLLTSYQSLLRVTKEK 2619
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKleELNERWEELLELAEER 205
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3069-3283 8.55e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.52  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3069 LQERFQKASRGFQQWLvNAKITTAKCFDLPQNLSEVSSSLQKIQEFLSESENGQHKLNTMLFKGELLSSLLTEEkAQAVQ 3148
Cdd:cd00176      1 KLQQFLRDADELEAWL-SEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3149 AKVLTAKEEWKSFHANLHQKESALENLKIQMKDFEVSAELVQnWLSKTERLVQeSSNRLYDLPAKRREQQKLQSVLEEIQ 3228
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076625 3229 CYEPQLHRLKEKARQLWEGQ--AASKSFVHRVSQLSSQYLALSNVTKEKVSRLDRII 3283
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
29-141 8.73e-06

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 48.42  E-value: 8.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   29 QKRTFTKWINSHLAKRKPPMVVDDLFEDMKDGIKLLALLEVLSGQKLPCEQGHRVKRIHAVANIGTALKFLEGRKsmyrg 108
Cdd:cd21285     11 DKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKG----- 85
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907076625  109 spIKLVNINATDIADGRPSIVLGLMWTIILYFQ 141
Cdd:cd21285     86 --INIQGLSAEEIRNGNLKAILGLFFSLSRYKQ 116
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
31-134 1.31e-05

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 47.80  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   31 RTFTKWINShlAKRKPPmvVDDLFEDMKDGIKLL-ALLEVLSGQ-------KLPCEQGhrVKRIHAVANIGTALKFLEGR 102
Cdd:cd21300     10 RVFTLWLNS--LDVEPA--VNDLFEDLRDGLILLqAYDKVIPGSvnwkkvnKAPASAE--ISRFKAVENTNYAVELGKQL 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907076625  103 KsmyrgspIKLVNINATDIADGRPSIVLGLMW 134
Cdd:cd21300     84 G-------FSLVGIQGADITDGSRTLTLALVW 108
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
23-137 1.66e-05

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 47.44  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   23 DEQEivqKRTFTKWINSHLA------KRKP-PMVVDDLFEDMKDGIKLLALL----------EVLSgqkLPCEQGHRVKR 85
Cdd:cd21294      4 NEDE---RREFTKHINAVLAgdpdvgSRLPfPTDTFQLFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPLNN 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907076625   86 IHAVANIGTALkflEGRKSMyrgsPIKLVNINATDIADGRPSIVLGLMWTII 137
Cdd:cd21294     78 FQMIENNNIVI---NSAKAI----GCSVVNIGAGDIIEGREHLILGLIWQII 122
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3288-3492 1.76e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 49.37  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3288 RFSQGVKELQDWMSDAVHMLDSYCLPtSDKSVLDSRMLKLEALLSVRQEKEIQMKMVVTRGEYVLQSTSlEGSAAVQQQL 3367
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3368 QAVKDMWESLLSAAIRCKSQLEGALSKWtSYQDDVRQFSSWMDSVEVSLTESEKQHtELREKITALGKAKLLNEEVLSHS 3447
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 3448 SLLETIEVKRAAMTEH------YVTQLELQDLQERHQALKEKAKEAVTKLE 3492
Cdd:cd00176    160 PRLKSLNELAEELLEEghpdadEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3497-3708 2.44e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.98  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3497 LHQEYQRDLKAFESWLEQEQEKLDRcSVHEGDTNAHETMLRDLQELQVRCAEGQALLNSVLHTREDVIPSGLPQAED--R 3574
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiqE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3575 VLESLRQDWQVYQHRLAEARMQLNNVVNKLrlmeQKFQQADEWLKRMEEKINFRSECQSSRSDKEIQLLQ--LKKWHEDL 3652
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQ----QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLkkHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907076625 3653 SAHRDEVEEVGTRAQGILDETHISSRMGCQAT--QLTSRYQALLLQVLEQIKFFEEEL 3708
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKleELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1255-2115 2.52e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1255 ISGPQESKEEAEMILDS--KNL---------LEAQQLLLHHQQKTKMISAKKRDLQEQMEQAQQGGQAGPGQEELRKLES 1323
Cdd:TIGR02168  167 ISKYKERRKETERKLERtrENLdrledilneLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1324 TLTGLEQSRERQERRIQVSLRKWERFETnketvvrylfQTGSSHERFLSFSSLESLSSELEQTKEfsKRTESIATQAENL 1403
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRL----------EVSELEEEIEELQKELYALANEISRLE--QQKQILRERLANL 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1404 VKEAAELPLGPRNkrvLQRQAKSIKEQVTTLEDTLEEDIKTMEMVKSKWDHFGSNFETLSIWILEKENELSSLEASASAA 1483
Cdd:TIGR02168  315 ERQLEELEAQLEE---LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1484 DVQISQIKVTIQEIESKIDSIvgleeeAQSFAQFVTTGESARIKAKLTQIRRYWEELQEHARGLEGTIlghlSQQQKFEE 1563
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERL------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ----EELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1564 NLRKIRQSVSEFAERLADpikicssaaeTYKVLQEHMDLCQAVESLSSTVTMFSASAQKAVNRESctqEAAALQQQYEEI 1643
Cdd:TIGR02168  462 ALEELREELEEAEQALDA----------AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS---GLSGILGVLSEL 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1644 LHKAKEMQTALEDLLAR----------------WQRLEKGLSPFLTWLErceaIASSPEKDISADRGKVESELQLIQALQ 1707
Cdd:TIGR02168  529 ISVDEGYEAAIEAALGGrlqavvvenlnaakkaIAFLKQNELGRVTFLP----LDSIKGTEIQGNDREILKNIEGFLGVA 604
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1708 NEVVSQASLYSNLLQLKEALFSVASKEDVAVMKLQLEQLDERwgdlpqIISKRMHFLQSVLAEHKQFDellfsfsvwiKQ 1787
Cdd:TIGR02168  605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYR------IVTLDGDLVRPGGVITGGSA----------KT 668
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1788 FLGELQRTSEInlrdhqvaltrhKDHAAEIEKKRGEITHLQGHLSQLRslgraQDLHPLQSKVDDCFQLFEEASQVVERR 1867
Cdd:TIGR02168  669 NSSILERRREI------------EELEEKIEELEEKIAELEKALAELR-----KELEELEEELEQLRKELEELSRQISAL 731
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1868 KLALAQLAEFLQSHACMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESSAISLDGTLTKAQCHLKSASpE 1947
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-A 810
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1948 ERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMDRErlkvptRQALQHRLRVFNQ 2027
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------ESELEALLNERAS 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2028 LEDELNSHEHELcwlkdkakqiaqkdvafaPEVDREINGLEATWDDTRRQIHENQGQccgLIDLVREYQSLKSTVCNVLE 2107
Cdd:TIGR02168  885 LEEALALLRSEL------------------EELSEELRELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQE 943

                   ....*...
gi 1907076625 2108 DASNVVVM 2115
Cdd:TIGR02168  944 RLSEEYSL 951
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4669-5426 6.91e-05

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: 50.06  E-value: 6.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4669 KTQEAILARKEYTSLIELTTQSLGDLEDQFLKMRKMpSDLIVEESVSLQQSCSALLGEVVALGEAVNELNQKKESFRSTG 4748
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEE-IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4749 QPWQ---PEKMLQLATLYHRLKRQAEQRVSFLEDTTSVYKEHAQMCRQLESQLEVVKREQAKVNEETLPAEEKLKVYHSL 4825
Cdd:TIGR02168  326 EELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4826 AGSLQDSGILLKRVATHLEDLSPHLDPTAYEKAKSQVQSWQEELKQMTSDVGELVTECESRMVQSIDFQTEMSRSLDWLR 4905
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4906 RVKAELSGPVCLDLSLQDIQEEIRKIQIHQEEVLSSLRIMSALSHKEqEKFTKAKEL-ISADLEHTLAELQELDGDVQEA 4984
Cdd:TIGR02168  486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD-EGYEAAIEAaLGGRLQAVVVENLNAAKKAIAF 564
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4985 LR-TRQATLTeiysrcqryyqvFQAANDWLDDaqemlQLAGNGLDV-ESAEENLRSHMEFFKTEGQFHSNMEELRGLVAR 5062
Cdd:TIGR02168  565 LKqNELGRVT------------FLPLDSIKGT-----EIQGNDREIlKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5063 LDPLikatgkeELAQKMASLEKRSQGIIQeshTQRDLLQRCMVQWQEYQKAREGVIELMNDAEKKLSEFAVLKtSSIHEA 5142
Cdd:TIGR02168  628 VDDL-------DNALELAKKLRPGYRIVT---LDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELE-EKIAEL 696
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5143 EEKLSKHKALVSVVDSFHEKIVALEEKASQlEQTGNDTSKATLSRSMTTVWQRWTRLRAVAQDQEKILEDAVDEWKRLSA 5222
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5223 KVKETTEVINQLQGRLPGSSTE-KASKAELMTLLESHDTYLMDLESQQLTLGVLQQRA------LSMLQDRAFPGTEEEV 5295
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEElKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrLEDLEEQIEELSEDIE 855
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5296 PILRAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYLGnptiEIDTQLEELKRLLAEATSHQ 5375
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQLELRL 931
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907076625 5376 ESIEKIAEEQKNKYLGLYTVLPSEISLQLAEVALDLkihDQIQEKVQEIEE 5426
Cdd:TIGR02168  932 EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE---EEARRRLKRLEN 979
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2520-2736 7.60e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 47.44  E-value: 7.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2520 ELGSFEDQHRKLNLWIHEMEERLKTENLGESKHHIsekKNEVRKVEMFLGELLAARESLDKLSQRGQLLSEESHSAGKG- 2598
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV---EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEi 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2599 GCRSTQLLTSYQSLLRVTKEKLRSCQLALKEHEALEEATQSM-WARVKdvqDRLACAESTLGNKETLEGRLSQIQDILLM 2677
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEqWLEEK---EAALASEDLGKDLESVEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 2678 KGEGEVKLNLAIGKGDQALRSSNKEGQQAIQDQLEMLKKAWAEAMNSAVHAQSTLESVI 2736
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3743-3923 9.31e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 47.44  E-value: 9.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3743 DESMMGKKLKTLEVLLKDMEKGHSLLKSAREKGERaMKFLAEHEAEALRK---EIHTYMEQLKNLTSTVRKEcmsLEKGL 3819
Cdd:cd00176     31 DLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQErleELNQRWEELRELAEERRQR---LEEAL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3820 HLAKEFSDKYKVLaQWMAEYQEILCTPEEPKmELYEKKAQLSKYKSLQQMVLSHEPSVTSVQEKSEALLELVQDQS---L 3896
Cdd:cd00176    107 DLQQFFRDADDLE-QWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAdeeI 184
                          170       180
                   ....*....|....*....|....*..
gi 1907076625 3897 KDKIQKLQSDFQDLCSRAKERVFSLEA 3923
Cdd:cd00176    185 EEKLEELNERWEELLELAEERQKKLEE 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5139-5804 1.30e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5139 IHEAEEKLSKHkALVSVVDSFHEKIVALEEKASQLEQTgndtsKATLSRSMTTVWQRWTRLRAVAQDQEKILEDAVDEWK 5218
Cdd:TIGR02168  218 LKAELRELELA-LLVLRLEELREELEELQEELKEAEEE-----LEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5219 RLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLLESH-DTYLMDLESQQLTLGVLQQRALSMLQdrAFPGTEEEVPI 5297
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKlDELAEELAELEEKLEELKEELESLEA--ELEELEAELEE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5298 L-RAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINS----VKSWVQETKDYLGNPTI----EIDTQLEELKRLL 5368
Cdd:TIGR02168  370 LeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrRERLQQEIEELLKKLEEaelkELQAELEELEEEL 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5369 AEATSHQESIEKIAEEQKNKYLGLYTVLPSEISlQLAEVALDLKIHDQIQEKVQEIEEGKAmsqefscKIQKVTKDLTTI 5448
Cdd:TIGR02168  450 EELQEELERLEEALEELREELEEAEQALDAAER-ELAQLQARLDSLERLQENLEGFSEGVK-------ALLKNQSGLSGI 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5449 LTKLKaktdDLVHAKAEHKM-----LGEELdgcNSKLME-LDAAIQTFSerhsqlgQPLAKKIGKLTELHQQTIRQAENR 5522
Cdd:TIGR02168  522 LGVLS----ELISVDEGYEAaieaaLGGRL---QAVVVEnLNAAKKAIA-------FLKQNELGRVTFLPLDSIKGTEIQ 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5523 LSKLNQALShMEEYNEMLETVRKWIEKAKVLVH---GNIAW----NSASQLQEQYILHQTLLEESGEIDSDLEAMAEKvq 5595
Cdd:TIGR02168  588 GNDREILKN-IEGFLGVAKDLVKFDPKLRKALSyllGGVLVvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGG-- 664
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5596 hlanvycTGKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTSPEVGRRSLKEQLch 5675
Cdd:TIGR02168  665 -------SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL-- 735
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5676 rQHLLSEMESLKPKMQAVQLCQSALRiPEDVVASLPLCHAALRLQEEASQLQHTAIQQCNIMQEAVVQYEQYKQEMKHLQ 5755
Cdd:TIGR02168  736 -ARLEAEVEQLEERIAQLSKELTELE-AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1907076625 5756 QLIEEAHREIEDKPVATSNIQELQAQIslhEELAQKIKGYQEQIDSLNS 5804
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRL---EDLEEQIEELSEDIESLAA 859
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1420-2034 1.39e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1420 LQRQAKsIKEQVTTLEDtlEEDIKTMEMVKSKWDHFGSNFETLSIWILEKENELSSLEASASAADVQISQIKVTIQEIES 1499
Cdd:COG1196    205 LERQAE-KAERYRELKE--ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1500 KIDSIVGLEEEAQsfaqfvttgesARIKAKLTQIRRYWEELQEHARglegtilghlsQQQKFEENLRKIRQSVSEFAERL 1579
Cdd:COG1196    282 ELEEAQAEEYELL-----------AELARLEQDIARLEERRRELEE-----------RLEELEEELAELEEELEELEEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1580 ADPIKICSSAAETYKVLQEHMDlcQAVESLSSTVtmfSASAQKAVNRESCTQEAAALQQQYEEILHKAKEMQTALEDLLA 1659
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELA--EAEEALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1660 RWQRLEKGLspfLTWLERCEAIASSPEKDISADRGKVESELQLIQALQNEVVSQASLYSNLLQLKEALFSVASKED--VA 1737
Cdd:COG1196    415 RLERLEEEL---EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeaAA 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1738 VMKLQLEQLDERWGDLPQIISKRMHFLQSVLAEHKQfDELLFSFSVWIKQFLGELQRTSEINLRDHQVA------LTRHK 1811
Cdd:COG1196    492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALAAALQNIVVEDDEVAaaaieyLKAAK 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1812 DHAAE------IEKKRGEITHLQGHLSQLRSLGRAQDLHPLQSKVDDCFQLFEEASQVVERRKLALAQLAEFLQSHAcms 1885
Cdd:COG1196    571 AGRATflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR--- 647
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1886 tLLYQLRQTVEATKSMSKKQSDSLKTDLHSAIQDVKTLESSAISLDGTLTKAQchlksaspeertscRATTDQLSLEVER 1965
Cdd:COG1196    648 -EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL--------------LAEEEEERELAEA 712
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 1966 IQNLLGTKQSEADALVALKEAFREQKEELLRSIEDIEERMDRERLKVPTRQALQHRLRvfnQLEDELNS 2034
Cdd:COG1196    713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE---RLEREIEA 778
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
191-284 2.17e-04

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 44.21  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  191 LLKWVQHTAGKQMGIE--VKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLED-AFTIAET--QLGIPRLLDP 265
Cdd:cd21218     15 LLRWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQAaeKLGCKYFLTP 94
                           90
                   ....*....|....*....
gi 1907076625  266 EDVdVDkPDEKSIMTYVAQ 284
Cdd:cd21218     95 EDI-VS-GNPRLNLAFVAT 111
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
24-136 2.50e-04

third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409147  Cd Length: 117  Bit Score: 44.15  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKrkpPMVvDDLFEDMKDGIKLLALLEVLsgqKLPCEQGHRVKRI---------------HA 88
Cdd:cd21298      2 IEETREEKTYRNWMNSLGVN---PFV-NHLYSDLRDGLVLLQLYDKI---KPGVVDWSRVNKPfkklganmkkiencnYA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907076625   89 VAnIGTALKFlegrksmyrgspiKLVNINATDIADGRPSIVLGLMWTI 136
Cdd:cd21298     75 VE-LGKKLKF-------------SLVGIGGKDIYDGNRTLTLALVWQL 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4892-5104 3.29e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4892 DFQTEMSRSLDWLRRVKAELSGPVcLDLSLQDIQEEIRKIQIHQEEVLSSLRIMSALsHKEQEKFTKAKELISADLEHTL 4971
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4972 AELQELDGDVQEALRTRQATLTEIYSRcQRYYQVFQAANDWLDDAQEMLQLAGNGLDVESAEENLRSHMEFFKTEGQFHS 5051
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 5052 NMEELRGLVARLDPLIKATGKEELAQKMASLEKRSQGIIQESHTQRDLLQRCM 5104
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
753-1006 3.56e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  753 QDLEDLEKRVPVMDAQYKmiAKKAHLFAKESPQEEANEMLTTM-----------SKLKEQLSKVKECCSPLLYEAQQLTV 821
Cdd:TIGR02168  677 REIEELEEKIEELEEKIA--ELEKALAELRKELEELEEELEQLrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  822 PLEELETQITSFYDSLGKINEILSVLEQEAqsstlfkqkhQELLASQENCKKSLTLIEKGSQSVQKLVTS---SQARKPW 898
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEI----------EELEAQIEQLKEELKALREALDELRAELTLlneEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  899 DHTKLQKQIADVHHAFQSMIKKTGDWKKHVEANSRLMKKFEESRAELEKVLRVAqegLEEKGDPEELLRRHTEFFSQLDQ 978
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907076625  979 RV------LNAFLKACDELTDILpEQEQQGLQEA 1006
Cdd:TIGR02168  902 ELreleskRSELRRELEELREKL-AQLELRLEGL 934
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
24-137 3.77e-04

third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409180  Cd Length: 134  Bit Score: 43.84  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINSHLAKRKppmvVDDLFEDMKDGIKLLALLEVLsgqKLPCEQgHRVKRiHAVANIGTALKFLEG-R 102
Cdd:cd21331     18 EGETREERTFRNWMNSLGVNPH----VNHLYGDLQDALVILQLYEKI---KVPVDW-NKVNK-PPYPKLGANMKKLENcN 88
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907076625  103 KSMYRG---SPIKLVNINATDIADGRPSIVLGLMWTII 137
Cdd:cd21331     89 YAVELGkhpAKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
30-76 4.20e-04

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 43.03  E-value: 4.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907076625   30 KRTFTKWINSHLAKRKppMVVDDLFEDMKDGIKLLALLEVLSGQKLP 76
Cdd:cd21221      3 VRVLTEWINEELADDR--IVVRDLEEDLFDGQVLQALLEKLANEKLE 47
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3394-3672 5.38e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3394 KWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALgkakllneevlshSSLLETIEVKRAAMTEhyvtqlELQDL 3473
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL-------------EEKLEELRLEVSELEE------EIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3474 QERHQALKEKakeaVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRcsvHEGDTNAHETMLRD-LQELQVRCAEGQAL 3552
Cdd:TIGR02168  287 QKELYALANE----ISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEkLEELKEELESLEAE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3553 LNSVLHTREDvipsglpqAEDRvLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEKINFRSECQ 3632
Cdd:TIGR02168  360 LEELEAELEE--------LESR-LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1907076625 3633 SSRSDKEIQ--LLQLKKWHEDLSAHRDEVEEVGTRAQGILDE 3672
Cdd:TIGR02168  431 EEAELKELQaeLEELEEELEELQEELERLEEALEELREELEE 472
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2312-2517 5.46e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.13  E-value: 5.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2312 QVERFVKDITAWLINVEESLTRCAQTETCEGLKKAKDIRKELQSQQNSITSTQEELNSLCR------KHHSVELESLGRA 2385
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNElgeqliEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2386 MTGLIKKHEATSQLCSQTQARIQDSLEKH-FSGSMKEFQEWfLGAKAAARESSNLTGDSQILEARLHNLQGVLDSLSDGQ 2464
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQqFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 2465 SKLDVVTQEGQTLYAHLPKQIVSSIQEQITKANEEFQAFLKQCLKEKQALQDC 2517
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5422-5760 1.03e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5422 QEIEEGKAMSQEFSCKIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPL 5501
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5502 AKKIGKLTELHQqtiRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKAKvlvhgniawnSASQLQEQYI--LHQTLLEE 5579
Cdd:TIGR02169  775 HKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL----------NRLTLEKEYLekEIQELQEQ 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5580 SGEIDSDLEAMAEKVQhlanvyctgKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTIL 5659
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIE---------NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5660 TSPEVGRRSLKEQLCHRQHLLSEMESLKPKMQAVQLCQSALripEDVVASLPLCHAALRLQEEASQLqhtAIQQCNIMQE 5739
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL---EDVQAELQRVEEEIRALEPVNML---AIQEYEEVLK 986
                          330       340
                   ....*....|....*....|....*
gi 1907076625 5740 AVVQYEQYKQ----EMKHLQQLIEE 5760
Cdd:TIGR02169  987 RLDELKEKRAkleeERKAILERIEE 1011
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4490-4666 1.38e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.97  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4490 PDDVSKQVKTCKTAQASLKTYQNEVTGLCAQGRELMKGiTKQEQEEVLGKLQELQTVYDTVLQKCSHRLQELEKSLVSRK 4569
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4570 HFkEDFDKACHWLKQADIVTFPEiNLMNEKTELHAQLDKYQSILEQSPEYENLLLTLQTTGQAMLPSLNEVDHSYLSEKL 4649
Cdd:cd00176    111 FF-RDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
                          170
                   ....*....|....*..
gi 1907076625 4650 SALPQQFNVIVALAKDK 4666
Cdd:cd00176    189 EELNERWEELLELAEER 205
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4144-4341 1.70e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.59  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4144 AELWIYLQDADQQLQNMKRRHTELEIniaQNMVMQVKDFIKQLQCKQVSVSTIVEKVDKLTKN--QESPEHKE-ITHLND 4220
Cdd:cd00176     10 DELEAWLSEKEELLSSTDYGDDLESV---EALLKKHEALEAELAAHEERVEALNELGEQLIEEghPDAEEIQErLEELNQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4221 QWQDLClqsdKLCAQREQDLQRTSSYHDHMRVVEAFLEKFTTEWDSLARSNAESTAIHLEALKKLALALQEEMYA----I 4296
Cdd:cd00176     87 RWEELR----ELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAheprL 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907076625 4297 DDLKDCKQKLIEQLGLDDRELVREQTSHLEQRWFQLQDLVKRKIQ 4341
Cdd:cd00176    163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4143-4439 1.90e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4143 KAELWIYL---QDADQQLQNMKRRHTELEINIAQNMVmQVKDFIKQLQCKQVSVSTIVEKVDKLTKNQESPEHKEITHLN 4219
Cdd:TIGR02169  222 EYEGYELLkekEALERQKEAIERQLASLEEELEKLTE-EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4220 DQwQDLCLQSDKLCAQREQDLQRTSsyhdhmRVVEAFLEKFTTEWDSLARSnaestaihLEALKKLALALQEEmyaIDDL 4299
Cdd:TIGR02169  301 AE-IASLERSIAEKERELEDAEERL------AKLEAEIDKLLAEIEELERE--------IEEERKRRDKLTEE---YAEL 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 4300 KDCKQKLIEQLGLDDRELvreqtshleQRWFQLQDLVKRKIQVSVTNLEELNVIQSRFQELMEWAEEQQPNIVEALKQsp 4379
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEF---------AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG-- 431
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 4380 ppgmaqhLLMDHLAICSELEAKQVLLKSLMKDADRVMADLGLNERKV---------IQKALSEAQKHVS 4439
Cdd:TIGR02169  432 -------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlkeeydrVEKELSKLQRELA 493
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1983-2200 1.97e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1983 LKEAFREQKEELLRSIEDIEERMDRERLkVPTRQALQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDR 2062
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2063 EINGLEATWDDTRRQIHENQGQCCGLIDLVREYQSLKStVCNVLEDASNVVVMRATIKDQGDLKWAFSKHETSRNEMNSK 2142
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907076625 2143 QKELDSFTSKGKHLLSELkkiHSGDFSLVKTDMESTLDKWLDVSERIEENMDMLRVSL 2200
Cdd:cd00176    159 EPRLKSLNELAEELLEEG---HPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
PLN02939 PLN02939
transferase, transferring glycosyl groups
2627-2871 2.22e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.89  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2627 LKEHEALEEATQSMWARVKDVQDRLACAESTLGNKETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNkegqQA 2706
Cdd:PLN02939   162 LTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEN----ML 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2707 IQDQLEMLKKawaeamnSAVHAQSTLESVIdqwndYLEK-KSQLEQWMESVDQRL----EHPLQLQP----GLKEKFSLL 2777
Cdd:PLN02939   238 LKDDIQFLKA-------ELIEVAETEERVF-----KLEKeRSLLDASLRELESKFivaqEDVSKLSPlqydCWWEKVENL 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2778 DH-FQSIVSEAEDHTGALQQlaakSRELYQKTQ--DESFKEAGQEELRTQFQDIMtvaKEKMRTVEDLVK--DHLM---- 2848
Cdd:PLN02939   306 QDlLDRATNQVEKAALVLDQ----NQDLRDKVDklEASLKEANVSKFSSYKVELL---QQKLKLLEERLQasDHEIhsyi 378
                          250       260
                   ....*....|....*....|....*
gi 1907076625 2849 --YLDAVQEFADWLHSAKEELHRWS 2871
Cdd:PLN02939   379 qlYQESIKEFQDTLSKLKEESKKRS 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3469-3666 2.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3469 ELQDLQERHQALkEKAKEAVTKLEKLVRLHQEYQRdlkafeswLEQEQEKLDRCsvheGDTNAHETMLRDLQELQVRCAE 3548
Cdd:COG4913    233 HFDDLERAHEAL-EDAREQIELLEPIRELAERYAA--------ARERLAELEYL----RAALRLWFAQRRLELLEAELEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3549 GQALLNSvLHTREDVIPSGLPQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEKINfr 3628
Cdd:COG4913    300 LRAELAR-LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP-- 376
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907076625 3629 secqSSRSDKEIQLLQLKKWHEDLSAHRDEVEEVGTRA 3666
Cdd:COG4913    377 ----ASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
SPEC smart00150
Spectrin repeats;
3929-4036 2.71e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 2.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  3929 EDYNTELQEVEKWLLQMSGRLVAPDLleMSSLETITQQLAHHKAMMEEIAGFEDRLDNLKAKGDTLIGQCPEHlqakqKQ 4008
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDL--GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-----AE 73
                            90       100
                    ....*....|....*....|....*...
gi 1907076625  4009 TVQAHLQGTKDSYSAICSTAQRVYRSLE 4036
Cdd:smart00150   74 EIEERLEELNERWEELKELAEERRQKLE 101
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
24-145 2.77e-03

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409178  Cd Length: 118  Bit Score: 41.12  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625   24 EQEIVQKRTFTKWINShlAKRKPpmVVDDLFEDMKDGIKLLALLEVLsgqKLPCEQGHRVKRIHAVanIGTALKFLE--- 100
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNP--YVNHLYSDLCDALVIFQLYEMT---RVPVDWGHVNKPPYPA--LGGNMKKIEncn 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907076625  101 -----GRKSmyrgSPIKLVNINATDIADGRPSIVLGLMWTIILYFQIEEL 145
Cdd:cd21329     73 yavelGKNK----AKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLNVL 118
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2738-2950 2.95e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.82  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2738 QWNDYLEKKSQLEQWMESVDQRL--EHPLQLQPGLKekfSLLDHFQSIVSEAEDHTGALQQLAAKSRELYQKTQDESFK- 2814
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLssTDYGDDLESVE---ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEi 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2815 EAGQEELRTQFQDIMTVAKEKMRTVEDLVKDHlMYLDAVQEFADWLHSAKEELHRwSDTSGDPSATQKKLLKIKELIDSR 2894
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907076625 2895 EIGAGRLSRVESLAPAVKQNTAASGCELLNSEMQALRADWRQWEDCLFQTQSSLES 2950
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5534-5762 2.98e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.82  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5534 EEYNEMLETVRKWIEKAKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQHL--ANVYCTGKLSQQVT 5611
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5612 QFGREMEELRQAIRVRLRNLQDAAKDMKKFEgELRNLQVALEQAQTILTSPEVGR--RSLKEQLCHRQHLLSEMESLKPK 5689
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907076625 5690 MQAvqlcqsalripedvvaslpLCHAALRLQEEASQLQHTAIQQcnIMQEAVVQYEQYKQEMKHLQQLIEEAH 5762
Cdd:cd00176    162 LKS-------------------LNELAEELLEEGHPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
5109-5549 2.99e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5109 EYQKAREGVIELMNDAEKKLSEFAVLKtssIHEAEEKLSKHKALvsvvDSFHEKIVALEEkasQLEQTGNDTSKaTLSRS 5188
Cdd:pfam05483  177 EREETRQVYMDLNNNIEKMILAFEELR---VQAENARLEMHFKL----KEDHEKIQHLEE---EYKKEINDKEK-QVSLL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5189 MTTVWQRWTRLRavaqDQEKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTE-KASKAELMTLLESHDTYLMDLES 5267
Cdd:pfam05483  246 LIQITEKENKMK----DLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKElEDIKMSLQRSMSTQKALEEDLQI 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5268 QQLTLGVLQQRALSMLQDRAFPGTEEEVpilrAITALQDQCLNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETK 5347
Cdd:pfam05483  322 ATKTICQLTEEKEAQMEELNKAKAAHSF----VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5348 DYLGNPTIEidtqLEELKRLLAEATS---HQESIEKIAEEQKNKYLGLYTVLPS------EISLQLAEVALDLKIH-DQI 5417
Cdd:pfam05483  398 KFKNNKEVE----LEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQArekeihDLEIQLTAIKTSEEHYlKEV 473
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5418 QEKVQEIEEGK-------AMSQEFSCKIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTF 5490
Cdd:pfam05483  474 EDLKTELEKEKlknieltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 5491 SERHSQLGQPLAKKIGKLTELHQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEK 5549
Cdd:pfam05483  554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
192-285 3.35e-03

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 40.36  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  192 LKWVQHTAGKqmgIEVKDFGKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRENLEDAFTIAEtQLGIPRLLDPEDVDVD 271
Cdd:cd21185      7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGK-SLGVEPVLTAEEMADP 82
                           90
                   ....*....|....
gi 1907076625  272 KPDEKSIMTYVAQF 285
Cdd:cd21185     83 EVEHLGIMAYAAQL 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5437-5661 5.19e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5437 KIQKVTKDLTTILTKLKAKTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSERHSQLGQPLAKKIGKLTELHQQtI 5516
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-L 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5517 RQAENRLSKLNQALSHMEEYNEMletvrkwiekaKVLVHGNIAWNSASQLQEQYILHQTLLEESGEIDSDLEAMAEKVQH 5596
Cdd:COG4942    100 EAQKEELAELLRALYRLGRQPPL-----------ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907076625 5597 LANVycTGKLSQQVTQFGREMEELRQAIRVRLRNLQDAAKDMKKFEGELRNLQVALEQAQTILTS 5661
Cdd:COG4942    169 LEAE--RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1987-2847 5.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1987 FREQKEELLRSIEDIEERMDR------------ERLKVPTRQALQHRlrvfnQLEDELNSHEHELCW--LKDKAKQIAQK 2052
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYK-----ELKAELRELELALLVlrLEELREELEEL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2053 DVAFAP------EVDREINGLEATWDDTRRQIHENQGQccgLIDLVREYQSLKSTVCNVLEDASNVVVMRATIKDQ---- 2122
Cdd:TIGR02168  245 QEELKEaeeeleELTAELQELEEKLEELRLEVSELEEE---IEELQKELYALANEISRLEQQKQILRERLANLERQleel 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2123 -GDLKWAFSKHETSRNEMNSKQKELDSFTSKGKHLLSELKKIHSgdfslVKTDMESTLDKWLDVSERIEENMDMLRVSL- 2200
Cdd:TIGR02168  322 eAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA-----ELEELESRLEELEEQLETLRSKVAQLELQIa 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2201 SIWDDVLSRKDEIEGwSNSSLPKLAENISNLNNSLRAEELLKELESEVKIKALkLEDLHSKINNLKELTKnpetptELQF 2280
Cdd:TIGR02168  397 SLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE-LEELQEELERLEEALE------ELRE 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2281 IEADLRQKLEHAKEITEEARGTLKDFTAQRTQVERFVKDITAW----------------LINVEESLTRC--------AQ 2336
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgilgvlseLISVDEGYEAAieaalggrLQ 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2337 TETCEGLKKAKDIrKELQSQQNSITSTQEELNSLCRKhhsvELESLGRAMTGLIKKHEATSQLCSQTQARIQDSLEKHFS 2416
Cdd:TIGR02168  549 AVVVENLNAAKKA-IAFLKQNELGRVTFLPLDSIKGT----EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG 623
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2417 GSM------------KEFQE---------------WFLGAKAAARESSNLTGDSQI--LEARLHNLQGVLDSLSDGQSKL 2467
Cdd:TIGR02168  624 GVLvvddldnalelaKKLRPgyrivtldgdlvrpgGVITGGSAKTNSSILERRREIeeLEEKIEELEEKIAELEKALAEL 703
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2468 DVVTQEGQTLYAHLPKQIvSSIQEQITKANEEFQAFLKQCLKEKQALQDCVSELGSFEDQHRKLNLWIHEMEERLKTenl 2547
Cdd:TIGR02168  704 RKELEELEEELEQLRKEL-EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--- 779
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2548 geskhHISEKKNEVRKVEMFLGELLAARESLDKLSQRGQLLSEESHsagkggcrstQLLTSYQSLLRVTKEKLRSCQLAL 2627
Cdd:TIGR02168  780 -----AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA----------NLRERLESLERRIAATERRLEDLE 844
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2628 KEHEALEEATQSMWARVKDVQDRLacaestlgnkETLEGRLSQIQDILLMKGEGEVKLNLAIGKGDQALRSSNKEgQQAI 2707
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELI----------EELESELEALLNERASLEEALALLRSELEELSEELRELESK-RSEL 913
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2708 QDQLEMLKkawaEAMNSAVHAQSTLESVIDQWNDYLEKKSQLEqwmesvdqrLEHPLQLQPGLKEKFSLLDHfqsivsEA 2787
Cdd:TIGR02168  914 RRELEELR----EKLAQLELRLEGLEVRIDNLQERLSEEYSLT---------LEEAEALENKIEDDEEEARR------RL 974
                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907076625 2788 EDHTGALQQL------------AAKSRELYQKTQDESFKEAgQEELRTQFQDIMTVAKEKMRTVEDLVKDHL 2847
Cdd:TIGR02168  975 KRLENKIKELgpvnlaaieeyeELKERYDFLTAQKEDLTEA-KETLEEAIEEIDREARERFKDTFDQVNENF 1045
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5502-5760 5.97e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5502 AKKIGKLTELHQQTIRQAENRLSKLNQALSHMEEYNEMLETVRKWIEKAKVLvhgniawnsaSQLQEqyiLHQTLLEESG 5581
Cdd:COG4913    203 FKPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIELL----------EPIRE---LAERYAAARE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5582 EIDsDLEAMAEKVQHLANVYCTGKLSQQVTQFGREMEELRQAIRvRLRNLQDAAKDmkkfegELRNLQVALEQAQtilts 5661
Cdd:COG4913    270 RLA-ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE-RLEARLDALRE------ELDELEAQIRGNG----- 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5662 pevGRR--SLKEQLCHRQHLLSEMEslKPKMQAVQLCQSA-LRIPEDVVASLPLCHAALRLQEEASQLQHTAIQQcniMQ 5738
Cdd:COG4913    337 ---GDRleQLEREIERLERELEERE--RRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LA 408
                          250       260
                   ....*....|....*....|..
gi 1907076625 5739 EAVVQYEQYKQEMKHLQQLIEE 5760
Cdd:COG4913    409 EAEAALRDLRRELRELEAEIAS 430
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1555-2095 7.81e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1555 LSQQQKFEENLRKIRQSVSEFAERLADPIKICSSAAETYKVLQEHMDLCQAVESLSSTVTMfsasaqkavnRESCTQEAA 1634
Cdd:TIGR00618  262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS----------RAKLLMKRA 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1635 ALQQQYEEILHKAKEMQTAL--EDLLARWQRLEKGLSPFLTWLERCEAIASSPEKDISADRGKVESELQLIQALQNEVVS 1712
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHsqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1713 QASLYSNLLQLKEalfsvaskeDVAVMKLQLEQLDERWGDLPQIISKRmhfLQSVLAEHKQFDELLFSFSVWIKQfLGEL 1792
Cdd:TIGR00618  412 IDTRTSAFRDLQG---------QLAHAKKQQELQQRYAELCAAAITCT---AQCEKLEKIHLQESAQSLKEREQQ-LQTK 478
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1793 QRTSEINLRDHQVALTRHKDHAAEIEKKRGEITHLQGHLSQLRSLGraQDLHPLQSKVDDCFQLFEEASQV--------- 1863
Cdd:TIGR00618  479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--PLTRRMQRGEQTYAQLETSEEDVyhqltserk 556
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1864 --------VERRKLALAQLAEFLQSHACMSTLLYQLRQTVEATKSMSKKQSDSLKTDLHsaIQDVKtLESSAISLDGTLT 1935
Cdd:TIGR00618  557 qraslkeqMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH--ALLRK-LQPEQDLQDVRLH 633
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 1936 KAQCH--------------LKSASPEERTSCRATTDQLSLEVERIQNLLGTKQSEADALVALKEAFrEQKEELLRSIEDI 2001
Cdd:TIGR00618  634 LQQCSqelalkltalhalqLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETH 712
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 2002 EERMDRER----LKVPTRQA-LQHRLRVFNQLEDELNSHEHELCWLKDKAKQIAQKDVAFAPEVDREINGLEATWDDTRR 2076
Cdd:TIGR00618  713 IEEYDREFneieNASSSLGSdLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
                          570
                   ....*....|....*....
gi 1907076625 2077 QIHENQGQCCGLIDLVREY 2095
Cdd:TIGR00618  793 LREEDTHLLKTLEAEIGQE 811
CH_PLS_FIM_rpt4 cd21220
fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
191-287 9.21e-03

fourth calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the fourth CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409069  Cd Length: 105  Bit Score: 39.18  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625  191 LLKWVQHT---AGKQMGIE-VKDfgKSWRTGLAFHSVIHAIQPELVDLEKVKTRSNRE----NLEDAFTIAEtQLGIPRL 262
Cdd:cd21220      6 ILAWANSKvreAGKSSPISsFKD--PSLSTGLFLLDLLAAIDPGAVDYDLVTEGETDEekeqNAKYAISLAR-KIGAVIF 82
                           90       100
                   ....*....|....*....|....*
gi 1907076625  263 LDPEDVDVDKPdeKSIMTYVAQFLT 287
Cdd:cd21220     83 LLWEDIVEVKP--KMILTFVASLMA 105
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
5067-5492 9.54e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5067 IKATGKEELAQKMASLEKRSQGI-------IQESHTQRDLLQRCMVQWQEYQKAREGVIELMNDAEKKLSEFA--VLKTS 5137
Cdd:COG4717     43 IRAMLLERLEKEADELFKPQGRKpelnlkeLKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReeLEKLE 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5138 SIHEAEEKLSKHKALVSVVDSFHEKIVALEEKASQLEQTGNDTSKAT-------------LSRSMTTVWQRWTRLRAVAQ 5204
Cdd:COG4717    123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEaelaelqeeleelLEQLSLATEEELQDLAEELE 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5205 DQEKILEDAVDEWKRLSAKVKETTEVINQLQGRLPGSSTEKASKAELMTLL-------------ESHDTYLMDLESQQLT 5271
Cdd:COG4717    203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggSLLSLILTIAGVLFLV 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5272 LGVLQQRALSMLQDRAFPGTE-EEVPILRAITALQDQclNMQEKVKNHGKLVKQELQEREAVETRINSVKSWVQETKDYl 5350
Cdd:COG4717    283 LGLLALLFLLLAREKASLGKEaEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL- 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 5351 gNPTIEIDTQLEELKRLLAEATSHQ-ESIEKIAE--EQKNKYLGLYTVLPSEISLQLAEVALDLKIHD--QIQEKVQEIE 5425
Cdd:COG4717    360 -EEELQLEELEQEIAALLAEAGVEDeEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELE 438
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076625 5426 EGKAMSQEfscKIQKVTKDLTTILTKLKA--KTDDLVHAKAEHKMLGEELDGCNSKLMELDAAIQTFSE 5492
Cdd:COG4717    439 EELEELEE---ELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3385-3658 9.80e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3385 KSQLEGALSKWTSYQDDVRQFSSWMDSVEVSLTESEKQHTELREKITALGKAklLNEEVLSHSSLLETIEVKRAAMTEhy 3464
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--EYELLAELARLEQDIARLEERRRE-- 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3465 vTQLELQDLQERHQALKEKAKEAVTKLEKLVRLHQEYQRDLKAFESWLEQEQEKLDRcsvhegdtnAHETMLRDLQELQV 3544
Cdd:COG1196    314 -LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---------AEAELAEAEEELEE 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076625 3545 RCAEGQALLNSVLHTREDVipsglpQAEDRVLESLRQDWQVYQHRLAEARMQLNNVVNKLRLMEQKFQQADEWLKRMEEK 3624
Cdd:COG1196    384 LAEELLEALRAAAELAAQL------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1907076625 3625 INfrsECQSSRSDKEIQLLQLKKWHEDLSAHRDE 3658
Cdd:COG1196    458 EE---ALLELLAELLEEAALLEAALAELLEELAE 488
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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