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Conserved domains on  [gi|2203400754|sp|Q69YQ0|]
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RecName: Full=Cytospin-A; AltName: Full=Renal carcinoma antigen NY-REN-22; AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1-like; Short=SPECC1-like protein

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
1005-1116 1.53e-81

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: 260.76  E-value: 1.53e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21199      1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21199     81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
500-801 1.80e-13

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: 75.09  E-value: 1.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  500 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  580 KAQLENEKQKVAELYS-IHNSGDKS--------DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDE 650
Cdd:TIGR02168  760 EAEIEELEERLEEAEEeLAEAEAEIeeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  651 YRAFQEEAKK----------QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKK 720
Cdd:TIGR02168  840 LEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  721 LQDQKHDMER-------EIKTLHRRLREEsaewrqFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLTK 790
Cdd:TIGR02168  920 LREKLAQLELrleglevRIDNLQERLSEE------YSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAIE 993
                          330
                   ....*....|.
gi 2203400754  791 ELEEIKSRKQE 801
Cdd:TIGR02168  994 EYEELKERYDF 1004
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
172-802 4.26e-05

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  172 DNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQ-- 249
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQar 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  250 --NTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK--LFGYQSLSPEITPGNQ-SDGGGTLTSSVEGSAPG---- 320
Cdd:pfam15921  310 nqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQfSQESGNLDDQLQKLLADlhkr 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  321 SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGipSIERSRKGSSG-NASEVSVACL 396
Cdd:pfam15921  390 EKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNESLEKVSSL 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  397 TERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFSRQIEYFRSLldehhis 476
Cdd:pfam15921  467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR------- 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  477 yvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIESEQKGKA 556
Cdd:pfam15921  526 --VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVGQHGRTAG 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---------SL 626
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdikqerdQL 658
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QEDLAHTRNDANRLQdaiakveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLH 706
Cdd:pfam15921  659 LNEVKTSRNELNSLS-------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  707 DNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQfqaDLQTAVVIANDIKSEAqEEIGDLKRRLHE--- 780
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQ---ELSTVATEKNKMAGEL-EVLRSQERRLKEkva 807
                          650       660
                   ....*....|....*....|....*.
gi 2203400754  781 ----AQEKNEKLTKELEEIKSRKQEE 802
Cdd:pfam15921  808 nmevALDKASLQFAECQDIIQRQEQE 833
PHA03247 super family cl33720
large tegument protein UL36; Provisional
827-992 1.74e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  827 LSRRSSTSSEPT---------------PTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGP 891
Cdd:PHA03247  2663 RPRRARRLGRAAqassppqrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  892 ISTSKPLTALSDKRPNYGEIPvqehllrtSSASRPASlPRVPAMESAKTLSVSRRSSEEVKRDiSAQEGASPASLMAMGT 971
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTT--------AGPPAPAP-PAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPPAAVL 2812
                          170       180
                   ....*....|....*....|.
gi 2203400754  972 TSPQLSLSSSPTASVTPTTRS 992
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTS 2833
 
Name Accession Description Interval E-value
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
1005-1116 1.53e-81

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: 260.76  E-value: 1.53e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21199      1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21199     81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1014-1117 3.91e-19

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: 83.88  E-value: 3.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKSTL- 1088
Cdd:pfam00307    4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPKVLi 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1089 ---DINEmvrterPDWQNVMLYVTAIYKYFET 1117
Cdd:pfam00307   84 epeDLVE------GDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1015-1108 2.38e-17

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: 78.51  E-value: 2.38e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  1015 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY----QELNSQDKRRNFMLAFQAAESVGIKSTL-- 1088
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLfe 80
                            90       100
                    ....*....|....*....|..
gi 2203400754  1089 --DINEMvrteRPDWQNVMLYV 1108
Cdd:smart00033   81 peDLVEG----PKLILGVIWTL 98
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1012-1117 1.69e-15

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 81.14  E-value: 1.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQN-IDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKST 1087
Cdd:COG5069    125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
                           90       100       110
                   ....*....|....*....|....*....|
gi 2203400754 1088 LDINEMVRTERPDWQNVMLYVTAIYKYFET 1117
Cdd:COG5069    205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
500-801 1.80e-13

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: 75.09  E-value: 1.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  500 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  580 KAQLENEKQKVAELYS-IHNSGDKS--------DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDE 650
Cdd:TIGR02168  760 EAEIEELEERLEEAEEeLAEAEAEIeeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  651 YRAFQEEAKK----------QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKK 720
Cdd:TIGR02168  840 LEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  721 LQDQKHDMER-------EIKTLHRRLREEsaewrqFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLTK 790
Cdd:TIGR02168  920 LREKLAQLELrleglevRIDNLQERLSEE------YSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAIE 993
                          330
                   ....*....|.
gi 2203400754  791 ELEEIKSRKQE 801
Cdd:TIGR02168  994 EYEELKERYDF 1004
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
528-803 8.68e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 8.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  528 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdksdiqd 607
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  608 lLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMK 687
Cdd:COG1196    304 -IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  688 ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEA 767
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2203400754  768 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
398-825 1.99e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 1.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHhiSY 477
Cdd:PRK03918   207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  478 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 553
Cdd:PRK03918   277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  554 GKAALAATLEEYKatvasdqiEMNRLKAQLENEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:PRK03918   353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  634 RNDANRLQDAIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERS------- 684
Cdd:PRK03918   418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  685 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:PRK03918   498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  738 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 799
Cdd:PRK03918   578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
                          490       500
                   ....*....|....*....|....*.
gi 2203400754  800 QEEERGRVYNYMNAVERDLAALRQGM 825
Cdd:PRK03918   657 SEEEYEELREEYLELSRELAGLRAEL 682
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
396-801 5.80e-07

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: 53.96  E-value: 5.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 457
Cdd:pfam05483  273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  458 HFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 524
Cdd:pfam05483  353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  525 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLENEKQKVAELYSIHNsgdksd 604
Cdd:pfam05483  433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  605 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKEte 682
Cdd:pfam05483  496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-- 572
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  683 rSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:pfam05483  573 -ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2203400754  763 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam05483  648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
604-737 4.23e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.98  E-value: 4.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDlDEKE 680
Cdd:cd22656     99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  681 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:cd22656    176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
172-802 4.26e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  172 DNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQ-- 249
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQar 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  250 --NTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK--LFGYQSLSPEITPGNQ-SDGGGTLTSSVEGSAPG---- 320
Cdd:pfam15921  310 nqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQfSQESGNLDDQLQKLLADlhkr 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  321 SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGipSIERSRKGSSG-NASEVSVACL 396
Cdd:pfam15921  390 EKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNESLEKVSSL 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  397 TERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFSRQIEYFRSLldehhis 476
Cdd:pfam15921  467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR------- 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  477 yvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIESEQKGKA 556
Cdd:pfam15921  526 --VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVGQHGRTAG 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---------SL 626
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdikqerdQL 658
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QEDLAHTRNDANRLQdaiakveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLH 706
Cdd:pfam15921  659 LNEVKTSRNELNSLS-------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  707 DNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQfqaDLQTAVVIANDIKSEAqEEIGDLKRRLHE--- 780
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQ---ELSTVATEKNKMAGEL-EVLRSQERRLKEkva 807
                          650       660
                   ....*....|....*....|....*.
gi 2203400754  781 ----AQEKNEKLTKELEEIKSRKQEE 802
Cdd:pfam15921  808 nmevALDKASLQFAECQDIIQRQEQE 833
PHA03247 PHA03247
large tegument protein UL36; Provisional
827-992 1.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  827 LSRRSSTSSEPT---------------PTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGP 891
Cdd:PHA03247  2663 RPRRARRLGRAAqassppqrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  892 ISTSKPLTALSDKRPNYGEIPvqehllrtSSASRPASlPRVPAMESAKTLSVSRRSSEEVKRDiSAQEGASPASLMAMGT 971
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTT--------AGPPAPAP-PAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPPAAVL 2812
                          170       180
                   ....*....|....*....|.
gi 2203400754  972 TSPQLSLSSSPTASVTPTTRS 992
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTS 2833
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
575-725 2.79e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 2.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754   575 EMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYraf 654
Cdd:smart00787  155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400754   655 qEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 725
Cdd:smart00787  221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
134-817 6.35e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 6.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  134 QSKKLPSAGQGANDMALAKRSRSRTATECDVRMS------KSKSDNQISDRAALEAKVKDLLTLAKTKDvEILHLRNELR 207
Cdd:TIGR00606  403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtiELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELR 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  208 DMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK 287
Cdd:TIGR00606  482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  288 LFGYQSLSPeitpgNQSDGGGTLtSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEvyQPLTSSDDALDAPS 367
Cdd:TIGR00606  562 LTSLLGYFP-----NKKQLEDWL-HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--QLSSYEDKLFDVCG 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  368 SSESEG-----IPSIERSRKGSSGNASEVSVacLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENeRLGEEK 442
Cdd:TIGR00606  634 SQDEESdlerlKEEIEKSSKQRAMLAGATAV--YSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL-RLAPDK 710
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  443 VILMESLCQQSDKlehfsrqieyfrslldehhisyvidedvksgrymeleqrymdlaenarfEREQLLGVQQHLSNTLKM 522
Cdd:TIGR00606  711 LKSTESELKKKEK-------------------------------------------------RRDEMLGLAPGRQSIIDL 741
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  523 AEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKaTVASDQIEMNRLKAQLENEKQKVAELYSIHNSGD- 601
Cdd:TIGR00606  742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDl 820
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  602 ----------KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD---AIAKVEDEYRAFQEeakkQIEDLNMT 668
Cdd:TIGR00606  821 drtvqqvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE----QLVELSTE 896
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKH-------------------DME 729
Cdd:TIGR00606  897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqdgkddylkQKE 976
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  730 REIKTLHRRLREESAEWRQFQADLQTavvIANDIKSEAQEE------IGDLKRR--LHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR00606  977 TELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnLTLRKREneLKEVEEELKQHLKEMGQMQVLQMK 1053
                          730
                   ....*....|....*.
gi 2203400754  802 EERGRVYNYMNAVERD 817
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRN 1069
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
396-592 3.83e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG4942     32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE--- 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 syVIDEDVKSGRYMELE--------------QRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKER 540
Cdd:COG4942    109 --LLRALYRLGRQPPLAlllspedfldavrrLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEE 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2203400754  541 SHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:COG4942    187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
 
Name Accession Description Interval E-value
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
1005-1116 1.53e-81

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: 260.76  E-value: 1.53e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21199      1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21199     81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
999-1117 9.49e-80

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: 256.15  E-value: 9.49e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  999 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQA 1078
Cdd:cd21256      1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2203400754 1079 AESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET 1117
Cdd:cd21256     81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
1005-1116 6.67e-73

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: 236.85  E-value: 6.67e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21257      1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21257     81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
1014-1115 3.09e-36

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: 132.47  E-value: 3.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINE 1092
Cdd:cd21200      3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
                           90       100
                   ....*....|....*....|....
gi 2203400754 1093 MVRTE-RPDWQNVMLYVTAIYKYF 1115
Cdd:cd21200     83 MVRMGnRPDWKCVFTYVQSLYRHL 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
1012-1115 7.61e-35

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: 129.02  E-value: 7.61e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21216     10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21216     90 EDIVNTPRPDERSVMTYVSCYYHAF 114
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
1012-1113 1.74e-32

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: 122.02  E-value: 1.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21259      1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKhADCPQLLDV 80
                           90       100
                   ....*....|....*....|...
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYK 1113
Cdd:cd21259     81 EDMVRMREPDWKCVYTYIQEFYR 103
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
1017-1115 1.06e-30

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: 116.76  E-value: 1.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRT 1096
Cdd:cd21198      6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
                           90
                   ....*....|....*....
gi 2203400754 1097 ERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21198     86 SVPDKLSVMTYLHQIRAHF 104
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
1008-1115 1.59e-30

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: 116.47  E-value: 1.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1008 EYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQ-AAESVGIKS 1086
Cdd:cd21291      6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
                           90       100
                   ....*....|....*....|....*....
gi 2203400754 1087 TLDINEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21291     86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
1012-1115 1.20e-29

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: 113.66  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLD- 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21194     81 AEDVDVARPDEKSIMTYVASYYHYF 105
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
1014-1113 3.02e-29

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: 112.87  E-value: 3.02e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVG-IKSTLDINE 1092
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
                           90       100
                   ....*....|....*....|.
gi 2203400754 1093 MVRTERPDWQNVMLYVTAIYK 1113
Cdd:cd21260     83 MVRMSVPDSKCVYTYIQELYR 103
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
1012-1115 5.58e-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: 112.02  E-value: 5.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21319      5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21319     84 PEDVFTENPDEKSIITYVVAFYHYF 108
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
1015-1115 8.37e-29

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: 111.22  E-value: 8.37e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1015 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEM 1093
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
                           90       100
                   ....*....|....*....|..
gi 2203400754 1094 VRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEAF 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
1016-1116 1.03e-28

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: 110.90  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1016 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEMV 1094
Cdd:cd21253      5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
                           90       100
                   ....*....|....*....|..
gi 2203400754 1095 RTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21253     85 ALKVPDKLSILTYVSQYYNYFH 106
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
1012-1115 1.21e-28

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: 110.95  E-value: 1.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21248     81 PEDVNVEQPDEKSIITYVVTYYHYF 105
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
1012-1115 1.75e-28

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: 110.52  E-value: 1.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21258      1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
                           90       100
                   ....*....|....*....|....*.
gi 2203400754 1091 NE-MVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21258     81 EDmMIMGKKPDSKCVFTYVQSLYNHL 106
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
1013-1115 8.44e-27

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: 105.70  E-value: 8.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1013 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDIN 1091
Cdd:cd21197      1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
                           90       100
                   ....*....|....*....|....
gi 2203400754 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21197     81 DMVTMHVPDRLSIITYVSQYYNHF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1012-1115 1.89e-26

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: 104.56  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21249      4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLDP 83
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 nEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21249     84 -EDVAVPHPDERSIMTYVSLYYHYF 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
1012-1116 1.93e-26

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: 104.48  E-value: 1.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDIN 1091
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1092 EMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21255     81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
1012-1115 3.34e-26

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: 103.89  E-value: 3.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESV-GIKSTLDI 1090
Cdd:cd21261      1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
                           90       100
                   ....*....|....*....|....*.
gi 2203400754 1091 NEM-VRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21261     81 EDMmVMGRKPDPMCVFTYVQSLYNHL 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
1017-1115 1.96e-25

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: 101.85  E-value: 1.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRT 1096
Cdd:cd21254      6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
                           90
                   ....*....|....*....
gi 2203400754 1097 ERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21254     86 AVPDKLTVMTYLYQIRAHF 104
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1012-1115 3.89e-24

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: 97.85  E-value: 3.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 nEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21189     81 -EDVDVPEPDEKSIITYVSSLYDVF 104
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
1013-1115 5.48e-24

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: 97.64  E-value: 5.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1013 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDIN 1091
Cdd:cd21250      5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
                           90       100
                   ....*....|....*....|....
gi 2203400754 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21250     85 EMASAEEPDKLSMVMYLSKFYELF 108
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
1014-1115 5.73e-24

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: 97.63  E-value: 5.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINE 1092
Cdd:cd21252      2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2203400754 1093 MVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21252     82 MVSMKVPDCLSIMTYVSQYYNHF 104
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
1010-1116 1.73e-23

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: 96.26  E-value: 1.73e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1010 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTL 1088
Cdd:cd21195      2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
                           90       100
                   ....*....|....*....|....*...
gi 2203400754 1089 DINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21195     82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
1017-1113 7.71e-23

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: 94.03  E-value: 7.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAA-ESVGIKSTLDiNEMVR 1095
Cdd:cd21187      5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
                           90
                   ....*....|....*...
gi 2203400754 1096 TERPDWQNVMLYVTAIYK 1113
Cdd:cd21187     84 VEQPDKKSILMYVTSLFQ 101
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
1012-1115 1.52e-22

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: 94.00  E-value: 1.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21287     10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21287     90 EDIVGTARPDEKAIMTYVSSFYHAF 114
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
1012-1116 3.38e-22

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: 92.70  E-value: 3.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21251      5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
                           90       100
                   ....*....|....*....|....*.
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21251     85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
1012-1115 1.92e-21

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: 90.89  E-value: 1.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21321      5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21321     84 PEDVNVDQPDEKSIITYVATYYHYF 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
1012-1115 3.02e-21

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: 90.52  E-value: 3.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21288     10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21288     90 EDIVNTPKPDERAIMTYVSCFYHAF 114
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
1012-1115 4.37e-21

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: 90.11  E-value: 4.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21322     17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21322     96 PEDVNMEAPDEKSIITYVVSFYHYF 120
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
1012-1115 5.54e-21

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: 89.78  E-value: 5.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21289     10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21289     90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
1012-1115 7.08e-21

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: 88.56  E-value: 7.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDIn 1091
Cdd:cd21240      4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDA- 82
                           90       100
                   ....*....|....*....|....
gi 2203400754 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21240     83 EDVDVPSPDEKSVITYVSSIYDAF 106
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
1012-1115 1.43e-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: 88.60  E-value: 1.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21290     13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21290     93 EDIVNTARPDEKAIMTYVSSFYHAF 117
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
1011-1116 2.51e-20

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: 87.09  E-value: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1011 GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
                           90       100
                   ....*....|....*....|....*..
gi 2203400754 1090 InEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21192     82 V-EDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
1012-1115 7.22e-20

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: 85.92  E-value: 7.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21320     81 PEDISVDHPDEKSIITYVVTYYHYF 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1014-1117 3.91e-19

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: 83.88  E-value: 3.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKSTL- 1088
Cdd:pfam00307    4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPKVLi 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2203400754 1089 ---DINEmvrterPDWQNVMLYVTAIYKYFET 1117
Cdd:pfam00307   84 epeDLVE------GDNKSVLTYLASLFRRFQA 109
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
1016-1115 2.54e-18

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: 81.36  E-value: 2.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1016 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEmV 1094
Cdd:cd21226      4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
                           90       100
                   ....*....|....*....|.
gi 2203400754 1095 RTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
1012-1115 2.96e-18

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: 81.19  E-value: 2.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDiN 1091
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
                           90       100
                   ....*....|....*....|....
gi 2203400754 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVF 103
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1015-1108 2.38e-17

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: 78.51  E-value: 2.38e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  1015 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY----QELNSQDKRRNFMLAFQAAESVGIKSTL-- 1088
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLfe 80
                            90       100
                    ....*....|....*....|..
gi 2203400754  1089 --DINEMvrteRPDWQNVMLYV 1108
Cdd:smart00033   81 peDLVEG----PKLILGVIWTL 98
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1014-1113 5.94e-17

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: 77.38  E-value: 5.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY---QELNSQDKRRNFMLAFQAAESVGIKST--L 1088
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1089 DINEMVrtERPDWQNVMLYVTAIYK 1113
Cdd:cd00014     81 EPEDLY--EKGNLKKVLGTLWALAL 103
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
1010-1115 2.02e-16

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: 76.20  E-value: 2.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1010 GGSKRnALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTL 1088
Cdd:cd21243      4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLL 82
                           90       100
                   ....*....|....*....|....*..
gi 2203400754 1089 DiNEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21243     83 D-PEDVDVDKPDEKSIMTYVAQFLKKY 108
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1012-1117 1.69e-15

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 81.14  E-value: 1.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQN-IDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKST 1087
Cdd:COG5069    125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
                           90       100       110
                   ....*....|....*....|....*....|
gi 2203400754 1088 LDINEMVRTERPDWQNVMLYVTAIYKYFET 1117
Cdd:COG5069    205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
1012-1115 4.74e-15

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: 71.88  E-value: 4.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQnidITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21184      1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
                           90       100
                   ....*....|....*....|....*.
gi 2203400754 1090 INEMVRTErPDWQNVMLYVTaiykYF 1115
Cdd:cd21184     78 PEDMVSPN-VDELSVMTYLS----YF 98
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
1017-1113 1.10e-14

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: 71.11  E-value: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKR-RNFMLAFQAAE-SVGIKSTLDiNEMV 1094
Cdd:cd21233      5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
                           90
                   ....*....|....*....
gi 2203400754 1095 RTERPDWQNVMLYVTAIYK 1113
Cdd:cd21233     84 ATAHPDKKSILMYVTSLFQ 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
500-801 1.80e-13

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: 75.09  E-value: 1.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  500 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  580 KAQLENEKQKVAELYS-IHNSGDKS--------DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDE 650
Cdd:TIGR02168  760 EAEIEELEERLEEAEEeLAEAEAEIeeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  651 YRAFQEEAKK----------QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKK 720
Cdd:TIGR02168  840 LEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  721 LQDQKHDMER-------EIKTLHRRLREEsaewrqFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLTK 790
Cdd:TIGR02168  920 LREKLAQLELrleglevRIDNLQERLSEE------YSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAIE 993
                          330
                   ....*....|.
gi 2203400754  791 ELEEIKSRKQE 801
Cdd:TIGR02168  994 EYEELKERYDF 1004
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
1012-1112 3.03e-13

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: 66.97  E-value: 3.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21238      2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
                           90       100
                   ....*....|....*....|..
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIY 1112
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLY 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
528-803 8.68e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 8.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  528 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdksdiqd 607
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  608 lLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMK 687
Cdd:COG1196    304 -IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  688 ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEA 767
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2203400754  768 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-804 1.00e-12

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: 72.78  E-value: 1.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  202 LRNELRDMRAQLGINEDHSEGDEKSEKETI---MAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGfSL 278
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEElkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-NE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  279 EQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSApgsvEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTS 358
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  359 SDDALDAPSSSESEGIPSIER---------SRKGSSGNASEVSVACLTERIHQMEENQHSTseELQATLQELADLQQITQ 429
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELqiaslnneiERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELE 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  430 ELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvidedvksgrYMELEQRYMDLAENARF---ER 506
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS---------------LERLQENLEGFSEGVKAllkNQ 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGA-----LKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKA 581
Cdd:TIGR02168  516 SGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  582 QLENEKQKVAELYSIHNSGDKSdIQDLLESVR-----------LDKEKAETLASSLQEDLAH------------------ 632
Cdd:TIGR02168  596 NIEGFLGVAKDLVKFDPKLRKA-LSYLLGGVLvvddldnalelAKKLRPGYRIVTLDGDLVRpggvitggsaktnssile 674
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  633 TRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNL 709
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  710 IISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEEAANLRERLESLE 830
                          650
                   ....*....|....*
gi 2203400754  790 KELEEIKSRKQEEER 804
Cdd:TIGR02168  831 RRIAATERRLEDLEE 845
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
1010-1099 1.19e-12

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: 65.45  E-value: 1.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1010 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTL 1088
Cdd:cd21196      1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
                           90
                   ....*....|.
gi 2203400754 1089 DINEMVRTERP 1099
Cdd:cd21196     81 SAQAVVAGSDP 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
604-799 1.44e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 72.26  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 DIQDLLESVRLDKEKAETLA--SSLQEDLAHTRNDANRLQDAIAKVEDeYRAFQ--EEAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4913    236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRL-WFAQRrlELLEAELEELRAELARLEAELERL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  680 ETERSDMKETIFELEDEVEQHravklhDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLR-------EESAEWRQFQAD 752
Cdd:COG4913    315 EARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAE 388
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2203400754  753 LQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:COG4913    389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
1012-1115 1.64e-12

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: 64.86  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21244      5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLE- 83
                           90       100
                   ....*....|....*....|....*
gi 2203400754 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVAQFLQYS 108
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
1017-1113 1.94e-12

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: 64.59  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDiNEMVR 1095
Cdd:cd21234      5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
                           90
                   ....*....|....*...
gi 2203400754 1096 TERPDWQNVMLYVTAIYK 1113
Cdd:cd21234     84 VQLPDKKSIIMYLTSLFE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
505-815 3.05e-12

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: 71.25  E-value: 3.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  505 EREQLLGVQQHLSNTLKMAEQDNKEAQEMIG--------------ALKERSHHMERIIESEQKGKAA-------LAATLE 563
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieqleqeeeKLKERLEELEEDLSSLEQEIENvkselkeLEARIE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  564 EYKATVASDQIEMNRLKA--------QLENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEArlshsripEIQAELSKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  636 DANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnLIIS 712
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEEleaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-------KRLS 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  713 DLENTVKKLQDQkhdmEREIKTLHRRLREESAEW---RQFQADLQ---TAVVIANDIKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:TIGR02169  921 ELKAKLEALEEE----LSEIEDPKGEDEEIPEEElslEDVQAELQrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
                          330       340
                   ....*....|....*....|....*....
gi 2203400754  787 KLTKELEEIKSRKQEEERGRVYNYMNAVE 815
Cdd:TIGR02169  997 KLEEERKAILERIEEYEKKKREVFMEAFE 1025
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
551-804 4.48e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 4.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  551 EQKGKA----ALAATLEEYKATVASDQIEmnRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:COG1196    207 RQAEKAeryrELKEELKELEAELLLLKLR--ELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLEL 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QE---DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAv 703
Cdd:COG1196    277 EElelELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  704 klhdnliisDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQE 783
Cdd:COG1196    352 ---------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
                          250       260
                   ....*....|....*....|.
gi 2203400754  784 KNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196    423 LEELEEALAELEEEEEEEEEA 443
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
567-821 4.87e-12

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: 70.48  E-value: 4.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  567 ATVASDQIEMNRLKAQLENEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQD 642
Cdd:TIGR02169  163 AGVAEFDRKKEKALEELEEVEENIERLDLIID--EKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  643 AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDM--------KETIFELEDEVEQHRAVKLHDNLIISDL 714
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  715 ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKRE 400
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2203400754  792 LEEIK---------SRKQEEERGRVYNYMNAVERDLAAL 821
Cdd:TIGR02169  401 INELKreldrlqeeLQRLSEELADLNAAIAGIEAKINEL 439
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
1015-1108 1.16e-11

second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 63.47  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1015 NALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQ--------------------------------E 1062
Cdd:cd21224      3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDairqpttqtvdraqdeaedfwvaefspstgdsG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2203400754 1063 LNSQDK---RRNFMLAFQAAESVGikstlDINEMVRTE-----RPDWQNVMLYV 1108
Cdd:cd21224     82 LSSELLaneKRNFKLVQQAVAELG-----GVPALLRASdmsntIPDEKVVILFL 130
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
1016-1115 1.38e-11

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: 62.12  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1016 ALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAA-ESVGIKSTLDiNEMV 1094
Cdd:cd21245      7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
                           90       100
                   ....*....|....*....|.
gi 2203400754 1095 RTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21245     85 MVDSPDEQSIMTYVAQFLEHF 105
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1015-1110 5.49e-11

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: 60.01  E-value: 5.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1015 NALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTyLPAHIP-YQELNSQDKRRNFMLAFQAAESVGIKSTLDINEM 1093
Cdd:cd21185      4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
                           90
                   ....*....|....*....
gi 2203400754 1094 VrteRPDWQN--VMLYVTA 1110
Cdd:cd21185     80 A---DPEVEHlgIMAYAAQ 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
396-803 1.24e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.85  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmeslcqqsdklehfSRQIeyfrslldehhi 475
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL---------------------SRQI------------ 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 syvidedvkSGRYMELEQrymdlaenARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKershhmERIIESEQKgK 555
Cdd:TIGR02168  729 ---------SALRKDLAR--------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE------EELAEAEAE-I 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  556 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS--GDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  634 RNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQhraVKLHDNLIISD 713
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSE----LEELSEELRELESKRSELRRELEELREKLAQ---LELRLEGLEVR 937
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  714 LENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLheaqeknEKLTKELE 793
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY-------DFLTAQKE 1010
                          410
                   ....*....|.
gi 2203400754  794 EI-KSRKQEEE 803
Cdd:TIGR02168 1011 DLtEAKETLEE 1021
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
398-825 1.99e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 1.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHhiSY 477
Cdd:PRK03918   207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  478 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 553
Cdd:PRK03918   277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  554 GKAALAATLEEYKatvasdqiEMNRLKAQLENEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:PRK03918   353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  634 RNDANRLQDAIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERS------- 684
Cdd:PRK03918   418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  685 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:PRK03918   498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  738 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 799
Cdd:PRK03918   578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
                          490       500
                   ....*....|....*....|....*.
gi 2203400754  800 QEEERGRVYNYMNAVERDLAALRQGM 825
Cdd:PRK03918   657 SEEEYEELREEYLELSRELAGLRAEL 682
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
529-804 4.04e-10

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: 64.32  E-value: 4.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  529 EAQEMIGALK-ERSHHMERIIESEQKGKAALAAtLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSihnsgDKSDIQD 607
Cdd:TIGR02169  678 RLRERLEGLKrELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-----DLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  608 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIA-----KVEDEYRAFQEEAKKQ----------IEDLNMTLEKL 672
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  673 RSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQAD 752
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  753 LQTAVVIANDIK---SEAQEEIGDLKRRLHEAQEKNEKlTKELEEIKSRKQEEER 804
Cdd:TIGR02169  912 IEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
396-822 5.10e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.91  E-value: 5.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhi 475
Cdd:PRK02224   326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG---- 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 syviDEDVKSGrymELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALK--------ERSHHMERI 547
Cdd:PRK02224   402 ----DAPVDLG---NAEDFLEELRE----ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETI 470
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  548 IESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaelysihnsgdksdiqdlLESVRLDKEKAETLASSLQ 627
Cdd:PRK02224   471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------------------IERLEERREDLEELIAERR 529
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  628 EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLnmtlEKLRSDLDEKETERSDMKETIFELEDEVEQHRAvklhd 707
Cdd:PRK02224   530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA----- 600
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  708 nliISDLENTVKKLQDQKHDMErEIKTLHR-RLREESAEWRQFQADLQTAvviandikseaqeeigdlkrRLHEAQEKNE 786
Cdd:PRK02224   601 ---IADAEDEIERLREKREALA-ELNDERReRLAEKRERKRELEAEFDEA--------------------RIEEAREDKE 656
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2203400754  787 KLTKELEEI--KSRKQEEERGRVYNYMNAVERDLAALR 822
Cdd:PRK02224   657 RAEEYLEQVeeKLDELREERDDLQAEIGAVENELEELE 694
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
613-823 6.18e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 6.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  613 RLDKEKAETLasslqEDLAHTRNDANRLQDAIAKVED-------------EYRAFQEEAKK--------QIEDLNMTLEK 671
Cdd:COG1196    169 KYKERKEEAE-----RKLEATEENLERLEDILGELERqleplerqaekaeRYRELKEELKEleaellllKLRELEAELEE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  672 LRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQA 751
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400754  752 DLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQ 823
Cdd:COG1196    324 ELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
609-804 1.11e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  609 LESVRLDKEKAE---TLASSLQE--------DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLD 677
Cdd:COG1196    202 LEPLERQAEKAEryrELKEELKEleaellllKLRELEAELEELEAELEELEAE----LEELEAELAELEAELEELRLELE 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  678 EKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG1196    278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2203400754  758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196    358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
412-824 1.31e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.78  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQITQELNSENERLGEEKvilmeslcqqsdklehfsRQIEYFRSLLDEHhisyvidEDVksgRYMEL 491
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRRER------------------EKAERYQALLKEK-------REY---EGYEL 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  492 EQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQkgkAALAATLEEYKATVAS 571
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  572 --DQIEMNRLKAQ-LENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:TIGR02169  306 leRSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  649 DEYRAFQEEakkqiedlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDM 728
Cdd:TIGR02169  385 DELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDK 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  729 EREIKTLHRRLREESAewrqfqadlqtavviandIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVY 808
Cdd:TIGR02169  447 ALEIKKQEWKLEQLAA------------------DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
                          410
                   ....*....|....*.
gi 2203400754  809 NYmnAVERDLAALRQG 824
Cdd:TIGR02169  509 GR--AVEEVLKASIQG 522
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
669-806 1.35e-09

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 62.18  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQ 748
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELTEEEEE---------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400754  749 FQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:COG2433    453 ARSEERREIRKDREISRL-DREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
387-797 1.90e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 61.96  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVIL---MESLCQQSDKLEHFSRQI 463
Cdd:TIGR04523  120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeKLNIQKNIDKIKNKLLKL 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  464 EYFRSLLDehhiSYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHH 543
Cdd:TIGR04523  200 ELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  544 MERI---IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYS-IHNSGDK-SDIQDLLESVRLDKEK 618
Cdd:TIGR04523  276 LEQNnkkIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNqISQNNKIiSQLNEQISQLKKELTN 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  619 AETLASSLQEDLahtrndaNRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELED 695
Cdd:TIGR04523  354 SESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  696 EVEQHRAVKLHDNLIISDLEN-------TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQ 768
Cdd:TIGR04523  427 EIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2203400754  769 ---EEIGDLKRRLHEAQEKNEKLTKELEEIKS 797
Cdd:TIGR04523  507 eleEKVKDLTKKISSLKEKIEKLESEKKEKES 538
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
387-822 2.17e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.98  E-value: 2.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  387 NASEVSVACLTERIHQMEENQhstsEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYF 466
Cdd:PRK02224   209 NGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  467 RSLLDEHhisyvidEDVKSGRYMELEQRYMDlAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 546
Cdd:PRK02224   285 RERLEEL-------EEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  547 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:PRK02224   357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-----PVDLGNAEDFLEELREERDELREREAEL 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QEDLAHTRND---ANRLQDA--------------IAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLD------EKETER 683
Cdd:PRK02224   432 EATLRTARERveeAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRI 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  684 SDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQADLQTAVVIA 760
Cdd:PRK02224   512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeeAREEVAELNSKLAELKERIESL 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  761 NDIKS------EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE--------------EERGRVYNYMNAVERDLAA 820
Cdd:PRK02224   592 ERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKREleaefdearieearEDKERAEEYLEQVEEKLDE 671

                   ..
gi 2203400754  821 LR 822
Cdd:PRK02224   672 LR 673
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
630-829 4.57e-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: 60.84  E-value: 4.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  630 LAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---------------------QIEDLNMTLEKLRSDLDEKETERSDMKE 688
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  689 TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTA---VVIANDIKS 765
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELA 340
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400754  766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGrvynyMNAVERDLAALRQGMGLSR 829
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLN 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
405-803 9.08e-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: 60.07  E-value: 9.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  405 ENQHSTSEELQATLQELADLQQITQELNSEnerlgeekvilMESLCQQSDKLEHFsrqIEYfRSLLDEHHISYVIDedvk 484
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERY---KEL-KAELRELELALLVL---- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  485 sgRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:TIGR02168  233 --RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  565 YKATVASDQIEMNRLKAQLENEKQKvaelysihnsgdksdiqdllesvrldKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESK--------------------------LDELAEELAELEEKLEELKEELESLEAEL 360
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  645 akveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQhravklhdnliisdLENTVKKLQDQ 724
Cdd:TIGR02168  361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--------------LEDRRERLQQE 422
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  725 KHDMEREIKTLHRR-LREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR02168  423 IEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
412-808 9.35e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.40  E-value: 9.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEdvKSGRYMEL 491
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE--LPERLEEL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  492 EQRYMDLAEnARFEREQLLGVQQHLSNTLKMAEQDNKEA--QEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATV 569
Cdd:COG4717    152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEE-LEEAQEELEELEEEL 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  570 asDQIEMNRLKAQLENEKQKVAELYSIHN-----SGDKSDIQDLLESV--------------RLDKEKAETLASSLQEDL 630
Cdd:COG4717    230 --EQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEEL 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  631 AHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKEtifeleDEVEQHRAVKLHDNLI 710
Cdd:COG4717    308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------EELEQEIAALLAEAGV 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  711 IS--DLENTVKKLQdQKHDMEREIKTLHRRLREESAEWRQFQADLQtavviandiKSEAQEEIGDLKRRLHEAQEKNEKL 788
Cdd:COG4717    382 EDeeELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
                          410       420
                   ....*....|....*....|
gi 2203400754  789 TKELEEIKSRKQEEERGRVY 808
Cdd:COG4717    452 REELAELEAELEQLEEDGEL 471
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
390-816 1.22e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  390 EVSVACLTERIHQMEENQHSTSEELQATLQELADLQQItQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSL 469
Cdd:PRK03918   251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  470 LDEhhisyvIDEDVK-----SGRYMELEQRYMDLAENAR-FEREQLLGVQ-------------QHLSNTLKMAEQDNKEA 530
Cdd:PRK03918   330 IKE------LEEKEErleelKKKLKELEKRLEELEERHElYEEAKAKKEElerlkkrltgltpEKLEKELEELEKAKEEI 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  531 QEMIGALKERSHHMERIIES---------EQKGKAAL----------AATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:PRK03918   404 EEEISKITARIGELKKEIKElkkaieelkKAKGKCPVcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  592 ELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqIEDLNMTLEK 671
Cdd:PRK03918   484 ELEKVLK--KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAE 560
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  672 LRSDLDEKETERSDMKETI----FELEDEVEQ---------HRAVKLHDnlIISDLENTVKKLQDQKHDMEREIKTL--- 735
Cdd:PRK03918   561 LEKKLDELEEELAELLKELeelgFESVEELEErlkelepfyNEYLELKD--AEKELEREEKELKKLEEELDKAFEELaet 638
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  736 ----------------------HRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLtkELE 793
Cdd:PRK03918   639 ekrleelrkeleelekkyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL--EKL 716
                          490       500
                   ....*....|....*....|...
gi 2203400754  794 EIKSRKQEEERGRVYNYMNAVER 816
Cdd:PRK03918   717 EKALERVEELREKVKKYKALLKE 739
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
387-699 1.51e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.31  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESlcqqsdKLEHFSRQIEYF 466
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE------KIGELEAEIASL 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  467 RSLLDehhisyvidedvksgrymELEQRYMDLAENARfereqllgvqqhlsntlkmaeqdnkEAQEMIGALKERSHHMER 546
Cdd:TIGR02169  307 ERSIA------------------EKERELEDAEERLA-------------------------KLEAEIDKLLAEIEELER 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  547 IIESEQKGKAALaatleeyKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDK--SDIQDLLESVRLDKEKAETLAS 624
Cdd:TIGR02169  344 EIEEERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQ 416
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQ 699
Cdd:TIGR02169  417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
575-823 2.03e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKAQLENEKQKVAELYSIHNSGD--KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAkvedEYR 652
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  653 AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEV---------------EQHRAVKLHDNLI------I 711
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleaeleeleaeleELESRLEELEEQLetlrskV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  712 SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2203400754  792 LEEIKSRKQEEERGRVynymnAVERDLAALRQ 823
Cdd:TIGR02168  463 LEELREELEEAEQALD-----AAERELAQLQA 489
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
620-823 2.32e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  620 ETLASSLQEDLAH---TRNDANRLQDAIAKVEDEYRAFQEEakkqIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE 696
Cdd:PRK02224   212 ESELAELDEEIERyeeQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  697 VEQHRAvKLHDNLIISDLEN-TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE------ 769
Cdd:PRK02224   288 LEELEE-ERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaa 366
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  770 ----EIGDLKRRLHEAQEKNEKLTKELEEIKSR--KQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:PRK02224   367 elesELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRE 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
399-778 2.42e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  399 RIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmeslcqqsdKLEHFSRQIEYfrslldehhisyv 478
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----------------RLELEELELEL------------- 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  479 ideDVKSGRYMELEQRYMDLAENARFEREQLlgvqQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAAL 558
Cdd:COG1196    284 ---EEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  559 AATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN 638
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  639 RLQDAIA--KVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE- 715
Cdd:COG1196    426 LEEALAEleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEg 505
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  716 -NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVV-IANDIKSEAQEEIGDLKRRL 778
Cdd:COG1196    506 fLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnIVVEDDEVAAAAIEYLKAAK 570
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
1012-1109 6.25e-08

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: 51.61  E-value: 6.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1012 SKRNALLKWCQKKTEGyqnIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
                           90       100
                   ....*....|....*....|
gi 2203400754 1090 INEMVrTERPDWQNVMLYVT 1109
Cdd:cd21230     78 PEEII-NPNVDEMSVMTYLS 96
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
649-803 6.32e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.93  E-value: 6.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  649 DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQK--H 726
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVRNNKeyE 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  727 DMEREIKTLHRRlreesaewrqfQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1579     93 ALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
397-802 1.74e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  397 TERIHQMEENQHSTSEELQATLQELADLQQITQELN--SENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhh 474
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  475 iSYVIDEDVKSGRYmELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKG 554
Cdd:COG4717    165 -LEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  555 K-----------AALAATLEEYKATVASDQIE------------------MNRLKAQLENEKQKVAELYSIHNsGDKSDI 605
Cdd:COG4717    243 ErlkearlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEE-LEEEEL 321
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSD 685
Cdd:COG4717    322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  686 MKETIFELEDEVEQHR--AVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADlqtavvianDI 763
Cdd:COG4717    400 LKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED---------GE 470
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2203400754  764 KSEAQEEIGDLKRRLHEAQEKN-------EKLTKELEEIKSRKQEE 802
Cdd:COG4717    471 LAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPP 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
399-696 3.52e-07

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: 54.69  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  399 RIHQMEENQHSTSEE-------LQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL-EHFSRQIEYFRSLL 470
Cdd:TIGR02169  724 EIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKL 803
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  471 DEHHISYvidedvkSGRYMELEQRymdlaENARFEREQLLgvqqhlsntlkmaEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:TIGR02169  804 EEEVSRI-------EARLREIEQK-----LNRLTLEKEYL-------------EKEIQELQEQRIDLKEQIKSIEKEIEN 858
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  551 EQKGKAALAATLEEYKATV-------ASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLA 623
Cdd:TIGR02169  859 LNGKKEELEEELEELEAALrdlesrlGDLKKERDELEAQLRELERKIEEL--------EAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  624 SSLQEDLAHTRN---------DANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLrSDLDEK----ETERSDMKETI 690
Cdd:TIGR02169  931 EELSEIEDPKGEdeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKraklEEERKAILERI 1009

                   ....*.
gi 2203400754  691 FELEDE 696
Cdd:TIGR02169 1010 EEYEKK 1015
46 PHA02562
endonuclease subunit; Provisional
575-809 4.56e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 53.86  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKaqleneKQKVAELYSihnsgdksDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI---AKVEDEY 651
Cdd:PHA02562   167 EMDKLN------KDKIRELNQ--------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYdelVEEAKTI 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  652 RAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR----------AVKLHDNLI------ISDLE 715
Cdd:PHA02562   233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqQISEGPDRItkikdkLKELQ 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  716 NTVKKLQDQKHDMER---EIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSE---AQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:PHA02562   313 HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDELDKIV 392
                          250       260
                   ....*....|....*....|
gi 2203400754  790 KELEEIKsrKQEEERGRVYN 809
Cdd:PHA02562   393 KTKSELV--KEKYHRGIVTD 410
PTZ00121 PTZ00121
MAEBL; Provisional
521-804 5.32e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 5.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  521 KMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATvASDQIEMNRLKAQLENEKQKVAELYSIHNSG 600
Cdd:PTZ00121  1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  601 DKSDIQDLLESVRLDKE--KAETLASSLQEDLAHTRNDANRLQDA--IAKVEDEYRAfqEEAKKQIEDLNMTLEKlRSDL 676
Cdd:PTZ00121  1510 KKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKA--EEAKKAEEDKNMALRK-AEEA 1586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  677 DEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADL 753
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2203400754  754 QTAVVIANDIKSEAQEEIGDlKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121  1667 AKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
396-801 5.80e-07

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: 53.96  E-value: 5.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 457
Cdd:pfam05483  273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  458 HFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 524
Cdd:pfam05483  353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  525 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLENEKQKVAELYSIHNsgdksd 604
Cdd:pfam05483  433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  605 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKEte 682
Cdd:pfam05483  496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-- 572
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  683 rSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:pfam05483  573 -ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2203400754  763 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam05483  648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
396-838 6.43e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 53.97  E-value: 6.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSE--ELQATL-----QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRS 468
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNEsnELHEKQkfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  469 LldehhisyviDEDVKSGRYMELEQ-RYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMiGALKERSHHMERI 547
Cdd:pfam15921  160 L----------KEDMLEDSNTQIEQlRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHF-RSLGSAISKILRE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  548 IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYSIHnsgdKSDIQDLLESVRLDKEKAETLASSLQ 627
Cdd:pfam15921  229 LDTEISYLKGRIFPVEDQLEALKSES--QNKIELLLQQHQDRIEQLISEH----EVEITGLTEKASSARSQANSIQSQLE 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  628 EDLAHTRND-------ANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQH 700
Cdd:pfam15921  303 IIQEQARNQnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  701 RAvKLHDNLIISDLENTV-KKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviandIKSEAQeeiGDLKRRLH 779
Cdd:pfam15921  383 LA-DLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA-------MKSECQ---GQMERQMA 451
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  780 EAQEKNE------KLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGMGLSRRS--STSSEPT 838
Cdd:pfam15921  452 AIQGKNEslekvsSLTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAieATNAEIT 520
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
499-764 7.57e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.84  E-value: 7.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  499 AENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKErshhMERIIESEQKGKAALAATLEEYKATVASDQIEMNR 578
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  579 LKAQLENEKQKVAE-LYSIHNSGDKSDIQDLLEsvrldkekaetlasslQEDLahtrNDANRLQDAiakvedeYRAFQEE 657
Cdd:COG4942     95 LRAELEAQKEELAElLRALYRLGRQPPLALLLS----------------PEDF----LDAVRRLQY-------LKYLAPA 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
                          250       260
                   ....*....|....*....|....*..
gi 2203400754  738 RLREESAEWRQFQADLQTAVVIANDIK 764
Cdd:COG4942    228 LIARLEAEAAAAAERTPAAGFAALKGK 254
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
619-895 7.63e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 7.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG3883     14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  699 QH-RAVKLHDNLI-----------ISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI 763
Cdd:COG3883     90 ERaRALYRSGGSVsyldvllgsesFSDFldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynymNAVERDLAALRQGMGLSRRSSTSSEPTPTVKT 843
Cdd:COG3883    170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA-------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2203400754  844 LIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883    243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
PTZ00121 PTZ00121
MAEBL; Provisional
359-791 8.32e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 8.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  359 SDDALDAPSSSESEGIPSIERSRKgssgnASEVSVACLTERIHQMEENQHSTSEEL----QATLQELADLQQITQELNSE 434
Cdd:PTZ00121  1536 ADEAKKAEEKKKADELKKAEELKK-----AEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  435 NERLGEEKVILMESLcqqsDKLEHFSRQIEYFRSLLDEHHISYvidEDVKSgrymELEQRYMDLAENARFEREQllgvqQ 514
Cdd:PTZ00121  1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKA---EELKK----AEEENKIKAAEEAKKAEED-----K 1674
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  515 HLSNTLKMAEQDNKEAQEMIGALKERSHHMERI--IESEQKGKAalaatlEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkKEAEEKKKA------EELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  593 LYSihNSGDKSDIQDLLE-----SVRLDKEKAETLASSLQEDLAHTRNDANRlqdAIAKVEDEYRAFQEEAKKQIEDLNm 667
Cdd:PTZ00121  1749 AKK--DEEEKKKIAHLKKeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIN- 1822
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  668 tleklrsdlDEKETERSDMKE------TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIktlhrrlrE 741
Cdd:PTZ00121  1823 ---------DSKEMEDSAIKEvadsknMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI--------E 1885
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  742 ESAEWRQFQADLQTAVVIANDIKSEAQEEIGD-------LKRRLHEAQEKNEKLTKE 791
Cdd:PTZ00121  1886 EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDkldkdeyIKRDAEETREEIIKISKK 1942
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
602-803 1.04e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  602 KSDIQDLLESVRLDK--EKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEeAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4717     36 KSTLLAFIRAMLLERleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEEL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  680 ETERSDMKETI--FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4717    115 REELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2203400754  758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG4717    195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
1017-1094 1.06e-06

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: 48.45  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWCQK--KTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIP----YQELNSQDKRRNFMLAFQAAESVGIKSTLDI 1090
Cdd:cd21218     15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94

                   ....
gi 2203400754 1091 NEMV 1094
Cdd:cd21218     95 EDIV 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
378-690 1.17e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 52.82  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  378 ERSRKGSSGNASEVsvacltERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLG-EEKVILMESLCQQSDKL 456
Cdd:pfam17380  299 ERLRQEKEEKAREV------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqEERKRELERIRQEEIAM 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  457 EhFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaENARFEREQLLGVQQhlsntlKMAEQDNKEAQEMIGA 536
Cdd:pfam17380  373 E-ISRMRELERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQ------IRAEQEEARQREVRRL 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  537 LKERSHHMERIIESEQKGKAALaatleeykATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDK 616
Cdd:pfam17380  441 EEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  617 EKAETLASSLQEdlahtRNDANRLQDAIAKVEDEYRAFQE-EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam17380  513 RKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
619-823 1.29e-06

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: 52.07  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  699 QHRavklhdnliisdlentvKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIA---NDIKSEAQEEIGDLK 775
Cdd:COG4942     94 ELR-----------------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylKYLAPARREQAEELR 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2203400754  776 RRLHEAQEKNEKLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:COG4942    157 ADLAELAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEK 206
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
415-792 1.42e-06

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: 52.66  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  415 QATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDE---------DVKS 485
Cdd:TIGR00618  337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRT 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  486 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHM---ERIIESEQKGKAALAATL 562
Cdd:TIGR00618  417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkEQIHLQETRKKAVVLARL 496
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  563 EEYK---------------ATVASDQIEMN-RLKAQLENEKQKVAElysihnSGDKSD--IQDLLESVRLDKEKAETLAS 624
Cdd:TIGR00618  497 LELQeepcplcgscihpnpARQDIDNPGPLtRRMQRGEQTYAQLET------SEEDVYhqLTSERKQRASLKEQMQEIQQ 570
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  625 SLQ----------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKE------ 688
Cdd:TIGR00618  571 SFSiltqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalha 650
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  689 TIFEL--EDEVEQHRAVKLHDNLIISDLENTVKKLQDQK-----------------HDMEREIKTLHRRLREESAEWRQF 749
Cdd:TIGR00618  651 LQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtllRELETHIEEYDREFNEIENASSSL 730
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2203400754  750 QADLQTAVVIANDIKSEAQEEIGD-LKRRLHEAQEKNEKLTKEL 792
Cdd:TIGR00618  731 GSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAAL 774
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
504-836 1.51e-06

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 52.27  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  504 FEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMERIIESEQKGKAaLAATLEEYKATV-ASDQIEMNRLK 580
Cdd:COG5185    193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIinIEEALKGFQDPESELED-LAQTSDKLEKLVeQNTDLRLEKLG 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  581 AQLENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQ-EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK 659
Cdd:COG5185    272 ENAESSKRLNEN-----ANNLIKQFENTKEKIAEYTKSIDIKKATESlEEQLAAAEAEQELEESKRETETGIQNLTAEIE 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  660 KQIEDLNMTLEKLRSDLDEKETER--SDMKETIFELEDEVE--------QHRAVKLHDNLIISDLENTVKKLQDQKHDME 729
Cdd:COG5185    347 QGQESLTENLEAIKEEIENIVGEVelSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  730 REIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRlhEAQEKNEKLTKELEEIKSRKQeEERGRVYN 809
Cdd:COG5185    427 RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR--SVRSKKEDLNEELTQIESRVS-TLKATLEK 503
                          330       340
                   ....*....|....*....|....*..
gi 2203400754  810 YMNAVERDLAALRQGMGLSRRSSTSSE 836
Cdd:COG5185    504 LRAKLERQLEGVRSKLDQVAESLKDFM 530
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
570-798 2.62e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 2.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  570 ASDQIEmnRLKAQLENEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLahtrnDANRLQDAIAKVED 649
Cdd:COG4913    608 NRAKLA--ALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  650 EYRAFQ------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV-----------------KLH 706
Cdd:COG4913    676 ELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelralleERF 755
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  707 DNLIISDLENTVKK-LQDQKHDMEREIKTLHRRLREE----SAEWRQFQADLQTAV-----------VIANDIKSEAQEE 770
Cdd:COG4913    756 AAALGDAVERELREnLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLeslpeylalldRLEEDGLPEYEER 835
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2203400754  771 igdLKRRLHEAQEK-----NEKLTKELEEIKSR 798
Cdd:COG4913    836 ---FKELLNENSIEfvadlLSKLRRAIREIKER 865
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
378-822 3.50e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  378 ERSRKGSSGNASEVSVACLTERIHQM-EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL 456
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  457 EHFSRQIEYFRSLLDEHHISYVIDEDVksgrYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGA 536
Cdd:TIGR02169  339 EELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  537 LKERSHHMERI---IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaELYSIHNsgDKSDIQDLLESVR 613
Cdd:TIGR02169  415 LQRLSEELADLnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE--EYDRVEKELSKLQ 489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  614 LDKEKAETLASSLQEDLAHTRNDANRLQDAI----------AKVEDEYRAFQE----------------EAKKQIEDLN- 666
Cdd:TIGR02169  490 RELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKr 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  667 -----MT---LEKLRSDldEKETERSDMKETIFELEDEVE---QHRAV---KLHDNLIISDLENT--------------- 717
Cdd:TIGR02169  570 rkagrATflpLNKMRDE--RRDLSILSEDGVIGFAVDLVEfdpKYEPAfkyVFGDTLVVEDIEAArrlmgkyrmvtlege 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  718 ----------------------------VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLqtavviandikSEAQE 769
Cdd:TIGR02169  648 lfeksgamtggsraprggilfsrsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-----------SDASR 716
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  770 EIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALR 822
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-----ENVKSELKELE 764
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
601-804 4.54e-06

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: 50.15  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  601 DKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLD 677
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleAELAELEKEIAELRAELE 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  678 EKETERSDMKETIFELEdeveQHRAVKLHdnLIISDLENTVKKLQDQKHdMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4942    101 AQKEELAELLRALYRLG----RQPPLALL--LSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAER 173
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2203400754  758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4942    174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
398-822 7.67e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 50.22  E-value: 7.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHS--------TSEELQA-TLQELAD--LQQITQELNSENERLGEekviLMESLCQQSDKLEHFSRQieyf 466
Cdd:pfam12128  471 ERIERAREEQEAanaeverlQSELRQArKRRDQASeaLRQASRRLEERQSALDE----LELQLFPQAGTLLHFLRK---- 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  467 RSLLDEHHISYVIDEdvksgrymELEQRyMDLaeNARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 546
Cdd:pfam12128  543 EAPDWEQSIGKVISP--------ELLHR-TDL--DPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  547 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSgdksdiqdllESVRLDKEKAETLASSL 626
Cdd:pfam12128  612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS----------EKDKKNKALAERKDSAN 681
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QE--DLAHTRNdanrlqdaiaKVEDEYRAFQEEAKKQIEDLNMT-LEKLRSDLDEKETERSDMKETIFELEdevEQHRAv 703
Cdd:pfam12128  682 ERlnSLEAQLK----------QLDKKHQAWLEEQKEQKREARTEkQAYWQVVEGALDAQLALLKAAIAARR---SGAKA- 747
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  704 klHDNLIISDLENTVKKL---QDQKHDMEREIKTLHRRL------REESAEWRQFQADL-----QTAVVIANDIKSEAQE 769
Cdd:pfam12128  748 --ELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIeriavrRQEVLRYFDWYQETwlqrrPRLATQLSNIERAISE 825
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  770 EIGDLKRRLHEAQEKNEKLTKELEeiKSRKQEEERGRVYNYMNAVERDLAALR 822
Cdd:pfam12128  826 LQQQLARLIADTKLRRAKLEMERK--ASEKQQVRLSENLRGLRCEMSKLATLK 876
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
412-681 7.96e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 7.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQAtlqELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHHISyvIDEDvkSGRYMEL 491
Cdd:PRK02224   478 EELEA---ELEDLEEEVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRET--IEEK--RERAEEL 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  492 EQRYMDLAENARFEREQLlgvqqhlsntlKMAEQDNKEAQEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATVAS 571
Cdd:PRK02224   543 RERAAELEAEAEEKREAA-----------AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIER 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  572 ------DQIEMNRL-KAQLENEKQKVAELYSIHNsgdksdiQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:PRK02224   611 lrekreALAELNDErRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2203400754  645 AKVEDEYRAFqEEAKKQIEDLNMTLEKLRSDLDEKET 681
Cdd:PRK02224   684 GAVENELEEL-EELRERREALENRVEALEALYDEAEE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
396-801 9.12e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 9.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI 475
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 SY------VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 549
Cdd:COG1196    387 ELlealraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  550 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAET-----LAS 624
Cdd:COG1196    467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAA 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  625 SLQEDLAHTRNDA------------------------------------------NRLQDAIAKVEDEYRAFQE------ 656
Cdd:COG1196    547 ALQNIVVEDDEVAaaaieylkaakagratflpldkiraraalaaalargaigaavDLVASDLREADARYYVLGDtllgrt 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  657 ---------------------EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE 715
Cdd:COG1196    627 lvaarleaalrravtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  716 NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTK----- 790
Cdd:COG1196    707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlla 786
                          490
                   ....*....|...
gi 2203400754  791 --ELEEIKSRKQE 801
Cdd:COG1196    787 ieEYEELEERYDF 799
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
512-678 1.15e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.00  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  512 VQQHLSNTLKMAEQDNKEAQemigALKERSHHMERIIESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:COG1579      2 MPEDLRALLDLQELDSELDR----LEHRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  592 E----LYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNM 667
Cdd:COG1579     77 KyeeqLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
                          170
                   ....*....|.
gi 2203400754  668 TLEKLRSDLDE 678
Cdd:COG1579    157 ELEELEAEREE 167
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
575-804 2.07e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKAQLENEKQKVAElysihnsgDKSDIQDLLESVRLDKEKAETLAS----------SLQEDLAHTRNDANRLQDAI 644
Cdd:TIGR04523  163 DLKKQKEELENELNLLEK--------EKLNIQKNIDKIKNKLLKLELLLSnlkkkiqknkSLESQISELKKQNNQLKDNI 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  645 AKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENtvKKL 721
Cdd:TIGR04523  235 EKKQQEINEKTTEisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-------ISDLNN--QKE 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  722 QDQKHDMEREIKTLHRRLREesaewrqfqadLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR04523  306 QDWNKELKSELKNQEKKLEE-----------IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374

                   ...
gi 2203400754  802 EER 804
Cdd:TIGR04523  375 LKK 377
COG5022 COG5022
Myosin heavy chain [General function prediction only];
491-968 2.97e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.54  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  491 LEQRYMDLAENARFEReQLLGVQQHLSNTLKmAEQDNKEAQEMIGALKERSHHmERIIESEQKGKAALaatLEEYKATVA 570
Cdd:COG5022    798 KLQPLLSLLGSRKEYR-SYLACIIKLQKTIK-REKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFS---LLKKETIYL 871
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  571 SDQIEMNRLKAQLENEKQKVAELYSIHNSGDKsdiqdlLESVRLdkEKAETLASSLQEDLAHTRNDANRLQDAIAKVE-D 649
Cdd:COG5022    872 QSAQRVELAERQLQELKIDVKSISSLKLVNLE------LESEII--ELKKSLSSDLIENLEFKTELIARLKKLLNNIDlE 943
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  650 EYRAFQEEAKKQIEDLNMtleklrsdldeketERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQ---DQKH 726
Cdd:COG5022    944 EGPSIEYVKLPELNKLHE--------------VESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYG 1009
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  727 DMEREIKTLHRRLREesaewrqfQADLQTAVVIANDIKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSR-----K 799
Cdd:COG5022   1010 ALQESTKQLKELPVE--------VAELQSASKIISSESTELSilKPLQKLKGLLLLENNQLQARYKALKLRRENsllddK 1081
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  800 QEEERGRVYNYMNAVERD--LAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNpaaaaiprtPLSPSPMKTPPA 877
Cdd:COG5022   1082 QLYQLESTENLLKTINVKdlEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVN---------TLEPVFQKLSVL 1152
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  878 -AAVSPMQRHSISGPISTSKPLTALSDKRpnygeiPVQEHLLRTSSASRPASLPrvpaMESAKTLSVSRRSSEEVKRDIS 956
Cdd:COG5022   1153 qLELDGLFWEANLEALPSPPPFAALSEKR------LYQSALYDEKSKLSSSEVN----DLKNELIALFSKIFSGWPRGDK 1222
                          490
                   ....*....|..
gi 2203400754  957 AQEGASPASLMA 968
Cdd:COG5022   1223 LKKLISEGWVPT 1234
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
1010-1110 3.79e-05

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: 44.00  E-value: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1010 GGSKRNALLKWCQKKTEgyqNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAEsvgikSTL 1088
Cdd:cd21315     14 GPTPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAE-----DWL 85
                           90       100
                   ....*....|....*....|....*..
gi 2203400754 1089 DINEMVRTE-----RPDWQNVMLYVTA 1110
Cdd:cd21315     86 DVPQLIKPEemvnpKVDELSMMTYLSQ 112
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
604-737 4.23e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.98  E-value: 4.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDlDEKE 680
Cdd:cd22656     99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  681 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:cd22656    176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
172-802 4.26e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  172 DNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQ-- 249
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQar 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  250 --NTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK--LFGYQSLSPEITPGNQ-SDGGGTLTSSVEGSAPG---- 320
Cdd:pfam15921  310 nqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQfSQESGNLDDQLQKLLADlhkr 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  321 SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGipSIERSRKGSSG-NASEVSVACL 396
Cdd:pfam15921  390 EKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNESLEKVSSL 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  397 TERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFSRQIEYFRSLldehhis 476
Cdd:pfam15921  467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR------- 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  477 yvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIESEQKGKA 556
Cdd:pfam15921  526 --VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVGQHGRTAG 586
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---------SL 626
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdikqerdQL 658
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  627 QEDLAHTRNDANRLQdaiakveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLH 706
Cdd:pfam15921  659 LNEVKTSRNELNSLS-------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  707 DNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQfqaDLQTAVVIANDIKSEAqEEIGDLKRRLHE--- 780
Cdd:pfam15921  732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQ---ELSTVATEKNKMAGEL-EVLRSQERRLKEkva 807
                          650       660
                   ....*....|....*....|....*.
gi 2203400754  781 ----AQEKNEKLTKELEEIKSRKQEE 802
Cdd:pfam15921  808 nmevALDKASLQFAECQDIIQRQEQE 833
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
575-819 4.61e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKAQLENEKQKVAELYS--------IHNSGDKSDIQDLLESVRLDKEKAE-TLASSLQEDLAHTRNDANRLQDAIA 645
Cdd:TIGR04523   41 KLKTIKNELKNKEKELKNLDKnlnkdeekINNSNNKIKILEQQIKDLNDKLKKNkDKINKLNSDLSKINSEIKNDKEQKN 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  646 KVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE--------------VEQHRAVKLHDN 708
Cdd:TIGR04523  121 KLEVELNKLEKQKKenkKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnllekeklniqknIDKIKNKLLKLE 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  709 LIISDLENTVKK---LQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKN 785
Cdd:TIGR04523  201 LLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2203400754  786 EK---LTKELEEIKSRKQEEERGRVYNYMNAVERDLA 819
Cdd:TIGR04523  281 KKikeLEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
mukB PRK04863
chromosome partition protein MukB;
604-807 5.03e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 DIQDLLESVRLDKEKAETLASSLQedlahtrndanRLQDAIAKVEDEYRAFQEEAKKqiedlnmtLEKLRSDLDEKETER 683
Cdd:PRK04863   891 TLADRVEEIREQLDEAEEAKRFVQ-----------QHGNALAQLEPIVSVLQSDPEQ--------FEQLKQDYQQAQQTQ 951
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  684 SDMKETIFELEDEVEQHRAVKLHDNLII----SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVI 759
Cdd:PRK04863   952 RDAKQQAFALTEVVQRRAHFSYEDAAEMlaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  760 ANDIKSEAQEEIGDLKRRLHE-----AQEKNEKLTKELEEIKSRKQEEERGRV 807
Cdd:PRK04863  1032 KRQMLQELKQELQDLGVPADSgaeerARARRDELHARLSANRSRRNQLEKQLT 1084
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
602-801 5.29e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  602 KSDIQDLLesvrldKEKAETLASSLQEdLAHTRNDANRLQDAIAKVEDEYRAFQE------EAKKQIEDLNMTLEKLRSD 675
Cdd:PRK03918   188 TENIEELI------KEKEKELEEVLRE-INEISSELPELREELEKLEKEVKELEElkeeieELEKELESLEGSKRKLEEK 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  676 LDEKETERSDMKETIFELEDEV-----------EQHRAVKLHDNLI---------ISDLENTVKKLQDQKHDME------ 729
Cdd:PRK03918   261 IRELEERIEELKKEIEELEEKVkelkelkekaeEYIKLSEFYEEYLdelreiekrLSRLEEEINGIEERIKELEekeerl 340
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400754  730 REIKTLHRRLREESAEWRQFQADLQTAVVIANDI----KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:PRK03918   341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
398-804 5.75e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 47.35  E-value: 5.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISY 477
Cdd:TIGR00606  301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  478 VIDE-------DVKSGRYMELEQRYM------------DLAENARFEREQL-------LGVQQHLSNTLKMAEQDNKEAQ 531
Cdd:TIGR00606  378 ELDGfergpfsERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQAdeirdekKGLGRTIELKKEILEKKQEELK 457
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  532 EMIGALKERSHHMERIIESEQKGKAALA--------ATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS 603
Cdd:TIGR00606  458 FVIKELQQLEGSSDRILELDQELRKAERelskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 -----DIQDLLESVRLDKEKAETLASSLQEDLAHT----------RNDANRLQDAIAKVEDEYrAFQEEAKKQIEDLNMT 668
Cdd:TIGR00606  538 emltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKkqledwlhskSKEINQTRDRLAKLNKEL-ASLEQNKNHINNELES 616
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  669 LEKLRSDLDEK-------ETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTlhrrlre 741
Cdd:TIGR00606  617 KEEQLSSYEDKlfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT------- 689
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  742 eSAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRR---------------------LHEAQEKNEKLTKELEEIKSRKQ 800
Cdd:TIGR00606  690 -EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlglapgrqsiidlkekeIPELRNKLQKVNRDIQRLKNDIE 768

                   ....
gi 2203400754  801 EEER 804
Cdd:TIGR00606  769 EQET 772
PRK01156 PRK01156
chromosome segregation protein; Provisional
363-822 6.73e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  363 LDAPSSSESEGIPSIER--------SRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNS- 433
Cdd:PRK01156   206 IADDEKSHSITLKEIERlsieynnaMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKi 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  434 ENERLGEEKVILMESLCQQSDkLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGR--YMELEQRYMDLAEnarfEREQLLG 511
Cdd:PRK01156   286 INDPVYKNRNYINDYFKYKND-IENKKQILSNIDAEINKYHAIIKKLSVLQKDYndYIKKKSRYDDLNN----QILELEG 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  512 VQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:PRK01156   361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  592 ELysihnsgdkSDIQDLLESVRLDKEKAETLASSLQEDLA-HTRNDANRLQDAIAKVEDEYRAFQEEAKKQI-------- 662
Cdd:PRK01156   441 EL---------SRNMEMLNGQSVCPVCGTTLGEEKSNHIInHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeyles 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  663 EDLNMT------LEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHD-----------NLIISDLEntVKKLQDQK 725
Cdd:PRK01156   512 EEINKSineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDldskrtswlnaLAVISLID--IETNRSRS 589
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  726 HDMEREIKTLHRRLREESAEWRQFQADLQTAV-VIANDIKS--EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRkqEE 802
Cdd:PRK01156   590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIrEIENEANNlnNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI--IP 667
                          490       500
                   ....*....|....*....|
gi 2203400754  803 ERGRVYNYMNAVERDLAALR 822
Cdd:PRK01156   668 DLKEITSRINDIEDNLKKSR 687
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
396-678 6.80e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--- 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 sYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERshhmERIIESEQKGK 555
Cdd:COG1196    321 -LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL----AEELLEALRAA 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  556 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2203400754  636 DANRLQDAIAKVEDEyrafqEEAKKQIEDLNMTLEKLRSDLDE 678
Cdd:COG1196    471 EAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLE 508
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
618-833 7.26e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 46.81  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  618 KAETLASSLQEDLaHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam07888   28 RAELLQNRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEeky 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  695 -------DEVEQHRAVKLHDN----LIISDLENTVKKLQDQKHDMEREI-------KTLHRRLREESAEWRQFQADLQTA 756
Cdd:pfam07888  104 kelsassEELSEEKDALLAQRaaheARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAKLQQT 183
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  757 VVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynyMNAVERDLAALRQGMGLSRRSST 833
Cdd:pfam07888  184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKVE 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
464-702 8.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  464 EYFRSL-LDEHHISYVIDEDVKS-GRYMELEQRymdlAENARFEREQLLGVQQHLSntlkmAEQDNKEAQEMIGALKERS 541
Cdd:COG4913    211 DFVREYmLEEPDTFEAADALVEHfDDLERAHEA----LEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAAL 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  542 HHMERiieseQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS---GDKSDIQDLLESVRLDKEK 618
Cdd:COG4913    282 RLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  619 AETLASSLQ--------------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtlekLRSDLDEKETERS 684
Cdd:COG4913    357 RERRRARLEallaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-------LRRELRELEAEIA 429
                          250
                   ....*....|....*...
gi 2203400754  685 DMKETIFELEDEVEQHRA 702
Cdd:COG4913    430 SLERRKSNIPARLLALRD 447
Rabaptin pfam03528
Rabaptin;
614-823 9.21e-05

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.25  E-value: 9.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYR--AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF 691
Cdd:pfam03528   13 LEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRqnAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  692 ELEDEVEqhravklhdnliiSDLENTVKKLQDQKHDMEREIK-TLHRRLREESAEWRQFqadlqtavviandiKSEAQEE 770
Cdd:pfam03528   93 EAIDEVK-------------SQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQY--------------RESAERE 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  771 IGDLKRRLHEAQEKnEKLTKELeeiksRKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:pfam03528  146 IADLRRRLSEGQEE-ENLEDEM-----KKAQEDAEKLRSVVMPMEKEIAALKA 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
606-895 1.15e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE---- 678
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaEIAEAEAEIEERREELGErara 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  679 --KETERSDMKETIF------ELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLhrrlreesaewRQFQ 750
Cdd:COG3883     95 lyRSGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-----------EALK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQGMGLSRR 830
Cdd:COG3883    164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA-----AAAAAAAAAAAAAAAAAAA 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  831 SSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883    239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
625-803 1.25e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.29  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR 701
Cdd:COG1340      5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaeKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  702 AVKlhdNLIISDLENtVKKLQDQKHDMEREIKTLHRRLREEsaEWRQfqadlQTAVVianDIKSEAQ--EEIGDLKRRLH 779
Cdd:COG1340     85 EKL---NELREELDE-LRKELAELNKAGGSIDKLRKEIERL--EWRQ-----QTEVL---SPEEEKElvEKIKELEKELE 150
                          170       180
                   ....*....|....*....|....*...
gi 2203400754  780 EAQ---EKNEKLTKELEEIKS-RKQEEE 803
Cdd:COG1340    151 KAKkalEKNEKLKELRAELKElRKEAEE 178
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
556-801 1.52e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  556 AALAATLEEYKATVASDQIEMNRLKAQLENEK-QKVAELYSIHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:pfam01576  225 AELQAQIAELRAQLAKKEEELQAALARLEEETaQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  634 RNDANRLQDAIAkVEDEYRAFQE----EAKKQIEDLNMTLEKLRSDLDEKETErsdmkeTIFELEDEVEQHRAVKlhdnl 709
Cdd:pfam01576  305 KTELEDTLDTTA-AQQELRSKREqevtELKKALEEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKRNK----- 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  710 iiSDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND---IKSEAQE-------EIGDLKRRLH 779
Cdd:pfam01576  373 --ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEklsklqsELESVSSLLN 450
                          250       260
                   ....*....|....*....|..
gi 2203400754  780 EAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam01576  451 EAEGKNIKLSKDVSSLESQLQD 472
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
513-806 1.61e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.97  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  513 QQH---LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQK-------GKAALAATLEEYKATVASDQIEMNRLKAQ 582
Cdd:pfam10174  323 KQHievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKqlqdlteEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  583 LENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI 662
Cdd:pfam10174  403 IENLQEQLRD-----KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  663 EDLNMTLEKLRSDLDEKETERSDMKE--------------TIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQ---- 724
Cdd:pfam10174  478 KDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEE-------CSKLENQLKKAHNAeeav 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  725 --KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI---KSEAQEEIGDLKRRlheAQEKNEKLTKELEEIKSRK 799
Cdd:pfam10174  551 rtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVeneKNDKDKKIAELESL---TLRQMKEQNKKVANIKHGQ 627

                   ....*..
gi 2203400754  800 QEEERGR 806
Cdd:pfam10174  628 QEMKKKG 634
PHA03247 PHA03247
large tegument protein UL36; Provisional
827-992 1.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  827 LSRRSSTSSEPT---------------PTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGP 891
Cdd:PHA03247  2663 RPRRARRLGRAAqassppqrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  892 ISTSKPLTALSDKRPNYGEIPvqehllrtSSASRPASlPRVPAMESAKTLSVSRRSSEEVKRDiSAQEGASPASLMAMGT 971
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTT--------AGPPAPAP-PAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPPAAVL 2812
                          170       180
                   ....*....|....*....|.
gi 2203400754  972 TSPQLSLSSSPTASVTPTTRS 992
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTS 2833
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1033-1097 1.75e-04

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: 41.99  E-value: 1.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400754 1033 ITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAesvgiKSTLDINEMVRTE 1097
Cdd:cd21229     21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLA-----KREFNIPMVLSPE 81
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
408-659 1.84e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  408 HSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvIDEDVKsgr 487
Cdd:COG4942     16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELA--- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  488 ymELEQRYMDLAENARFEREQLlgvQQHLSNTLKMAEQDNKE---AQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:COG4942     87 --ELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  565 YKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEdlahtrnDANRLQDAI 644
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQ-------EAEELEALI 229
                          250
                   ....*....|....*
gi 2203400754  645 AKVEDEYRAFQEEAK 659
Cdd:COG4942    230 ARLEAEAAAAAERTP 244
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
635-802 2.14e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  635 NDANRLQDAIAKVEDEYRAfQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF-ELEDEVEQH-RAVKLHDNLIIS 712
Cdd:PRK00409   513 EDKEKLNELIASLEELERE-LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAiKEAKKEADEIIK 591
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  713 DLENTVKKLQ-DQKhdmEREIKTLHRRLRE-----------ESAEWRQFQA--------DLQTAVVIANDIKSEAQEEIG 772
Cdd:PRK00409   592 ELRQLQKGGYaSVK---AHELIEARKRLNKanekkekkkkkQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAG 668
                          170       180       190
                   ....*....|....*....|....*....|
gi 2203400754  773 DLKRRLHEAQEknEKLTKELEEIKSRKQEE 802
Cdd:PRK00409   669 IMKMKVPLSDL--EKIQKPKKKKKKKPKTV 696
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
655-825 2.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  655 QEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDMEREIKT 734
Cdd:COG4717     76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  735 LHRRLREesaeWRQFQADLQTAvviANDIKsEAQEEIGDLKRRLHEAQEKN-EKLTKELEEIKSRKQ--EEERGRVYNYM 811
Cdd:COG4717    151 LEERLEE----LRELEEELEEL---EAELA-ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAelEEELEEAQEEL 222
                          170
                   ....*....|....
gi 2203400754  812 NAVERDLAALRQGM 825
Cdd:COG4717    223 EELEEELEQLENEL 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
658-804 2.25e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLII--SDLENTVKKLQDQKHDMEREIKTL 735
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL 687
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  736 hRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4913    688 -AALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
520-803 2.33e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 45.23  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  520 LKMAEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAATLEEYKAtvASDQIEMNR---------LKAQLENE 586
Cdd:pfam06160   81 FKKAKKALDEIEELLDDIEEDIKQIleelDELLESEEKNREEVEELKDKYRE--LRKTLLANRfsygpaideLEKQLAEI 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  587 KQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDanrLQDAIAKVEDEYRAFQEE--------- 657
Cdd:pfam06160  159 EEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE---LPDQLEELKEGYREMEEEgyalehlnv 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  658 ------AKKQIEDLNMTLEKLrsDLDEKETERSDMKETIFEL----EDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHD 727
Cdd:pfam06160  236 dkeiqqLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  728 MEREIKTLHrrLRE-ESAEWRQFQADLQTAV----VIANDIK------SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIk 796
Cdd:pfam06160  314 LERVQQSYT--LNEnELERVRGLEKQLEELEkrydEIVERLEekevaySELQEELEEILEQLEEIEEEQEEFKESLQSL- 390

                   ....*..
gi 2203400754  797 sRKQEEE 803
Cdd:pfam06160  391 -RKDELE 396
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
651-801 2.41e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  651 YRAFQEEAKKQIEDLNMTLEK-------LRSDLD------EKETERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENT 717
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRledilneLERQLKslerqaEKAERYKELKAELRELELALLVLRLEELREEL--EELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  718 VKKLQDQKHDMEREIKTLH---RRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                   ....*..
gi 2203400754  795 IKSRKQE 801
Cdd:TIGR02168  328 LESKLDE 334
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
538-804 2.50e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 45.12  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  538 KERSHHMERIiESEQKGkAALAATLEEYKATVASDQIEMNRLKAQlENEKQKVaelysihnsgdksdIQDLLESVRLDKE 617
Cdd:pfam05557   21 MELEHKRARI-ELEKKA-SALKRQLDRESDRNQELQKRIRLLEKR-EAEAEEA--------------LREQAELNRLKKK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  618 KAETLASSLQEDLAhTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam05557   84 YLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqq 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  695 ----------DEVEQHRAVKLHDNLIIsdleNTVKKLQDQKHDMEREIKtlhrRLREESAEWRQFQADlqtavviandiK 764
Cdd:pfam05557  163 sslaeaeqriKELEFEIQSQEQDSEIV----KNSKSELARIPELEKELE----RLREHNKHLNENIEN-----------K 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2203400754  765 SEAQEEIGDLKRRLH---EAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05557  224 LLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVK 266
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
575-725 2.79e-04

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 2.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754   575 EMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYraf 654
Cdd:smart00787  155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400754   655 qEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 725
Cdd:smart00787  221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
484-823 3.25e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  484 KSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIEseqkgKAALAATLE 563
Cdd:COG4717     61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELE 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  564 EYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdKSDIQDLLEsvRLDKEKAETLASSLQEdLAHTRNDANRLQDA 643
Cdd:COG4717    136 ALEAELAELPERLEELEERLEELRELEEELEEL-----EAELAELQE--ELEELLEQLSLATEEE-LQDLAEELEELQQR 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  644 IAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDL-DEKETERSDMKETIFELEDEVEQHRAVKLHDN-------------- 708
Cdd:COG4717    208 LAELEEEL----EEAQEELEELEEELEQLENELeAAALEERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvl 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  709 -LIISDLENTVKKLQDQKHDMErEIKTLHRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEK 787
Cdd:COG4717    284 gLLALLFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALGLP-------PDLSPEELLELLDRIEELQELLRE 355
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2203400754  788 LTKELEEIKSRKQEEERGRVYNYMNAveRDLAALRQ 823
Cdd:COG4717    356 AEELEEELQLEELEQEIAALLAEAGV--EDEEELRA 389
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
412-801 3.28e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQitqELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHhisyvideDVKSGRYMEL 491
Cdd:pfam10174  331 ESLTAKEQRAAILQT---EVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML--------DVKERKINVL 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  492 EQRYMDLAENARFEREQLLGvqqhLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKA----ALAATLEEYKA 567
Cdd:pfam10174  400 QKKIENLQEQLRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREredrERLEELESLKK 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  568 TVASDQIEMNRLKAQLENEKQKVAEL----YSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANR---- 639
Cdd:pfam10174  476 ENKDLKEKVSALQPELTEKESSLIDLkehaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpe 555
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  640 LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRsdldEKETERSDMKETIFELEDEVEQHravklhdnliISDLENTVK 719
Cdd:pfam10174  556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAELESLTLRQ----------MKEQNKKVA 621
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  720 KLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSeaQEEIGDLKRRLHEAQ----EKNEKLT------ 789
Cdd:pfam10174  622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQqslaEKDGHLTnlraer 699
                          410
                   ....*....|...
gi 2203400754  790 -KELEEIKSRKQE 801
Cdd:pfam10174  700 rKQLEEILEMKQE 712
PRK09039 PRK09039
peptidoglycan -binding protein;
575-693 4.46e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.80  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKAQLenekQKVAELYSIHNSGdKSDIQDLLESVRLDKEKAETLASSLQ---EDLAHTRNDANRLQDAIAKVEDEY 651
Cdd:PRK09039    54 ALDRLNSQI----AELADLLSLERQG-NQDLQDSVANLRASLSAAEAERSRLQallAELAGAGAAAEGRAGELAQELDSE 128
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2203400754  652 RAFQEEAKKQIEDLNMTLEKLRSD-------LDEKETERSDMKETIFEL 693
Cdd:PRK09039   129 KQVSARALAQVELLNQQIAALRRQlaaleaaLDASEKRDRESQAKIADL 177
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
396-803 4.92e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQ---QITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDE 472
Cdd:TIGR00618  206 LTLCTPCMPDTYHERKQVLEKELKHLREALqqtQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  473 -----------HHISYVIDEDVKSGRYMELEQRYMDLAENARFER------EQLLGVQQHLSNTLKMAEQDNKEAQE--- 532
Cdd:TIGR00618  286 inrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEvat 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  533 MIGALKERSHHMERIIESEQKGKAALAATLEEYKAtvasdqiemnrLKAQLENEKQKVAELYSIHNSgDKSDIQDLLESV 612
Cdd:TIGR00618  366 SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK-----------ELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQ 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  613 RLDKEKAETLASSLQedlahtrndaNRLQDAIAKVEDEYRAFQeeAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFE 692
Cdd:TIGR00618  434 ELQQRYAELCAAAIT----------CTAQCEKLEKIHLQESAQ--SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  693 LEDEVEQ---HRAVKLHDNLI-------ISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:TIGR00618  502 EPCPLCGsciHPNPARQDIDNpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2203400754  763 IKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR00618  582 SKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
505-792 5.11e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.44  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  505 EREQLLGVQQHlSNTLKMAEQdnkEAQEMIGALKErshhMERIIESEQKgkaALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:pfam12128  239 IRPEFTKLQQE-FNTLESAEL---RLSHLHFGYKS----DETLIASRQE---ERQETSAELNQLLRTLDDQWKEKRDELN 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  585 NEKQKVAELYSihnsGDKSDIqDLLES--VRLDKEKAETLASSlQEDLAHTRNDANR-------LQDAIAKVEDEYRAFQ 655
Cdd:pfam12128  308 GELSAADAAVA----KDRSEL-EALEDqhGAFLDADIETAAAD-QEQLPSWQSELENleerlkaLTGKHQDVTAKYNRRR 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  656 ----EEAKKQIEDLNMTLEKLRSDLD-EKETERSDMKETIFELEDEVEQH-RAVKLHDNLIISDLE------NTVKKLQD 723
Cdd:pfam12128  382 skikEQNNRDIAGIKDKLAKIREARDrQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGelklrlNQATATPE 461
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  724 QKHDMEREIKTLHRrLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL 792
Cdd:pfam12128  462 LLLQLENFDERIER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
Filament pfam00038
Intermediate filament protein;
597-825 5.41e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  597 HNSGDKSDIQDLLE----SVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI---EDLNMTL 669
Cdd:pfam00038   26 QNKLLETKISELRQkkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELnlrTSAENDL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  670 EKLRSDLDEKETERSDMKETIFELEDEVEQHRavKLHDNLIiSDLENTVKKLQDQ-------KHDME---REIKTLH--- 736
Cdd:pfam00038  106 VGLRKDLDEATLARVDLEAKIESLKEELAFLK--KNHEEEV-RELQAQVSDTQVNvemdaarKLDLTsalAEIRAQYeei 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  737 -RRLREESAEWRQFQ-ADLQTAVVIANDIKSEAQEEIGDLKRRLH------EAQEK-NEKLTKELEEIKSRkQEEERGRV 807
Cdd:pfam00038  183 aAKNREEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQsleielQSLKKqKASLERQLAETEER-YELQLADY 261
                          250
                   ....*....|....*...
gi 2203400754  808 YNYMNAVERDLAALRQGM 825
Cdd:pfam00038  262 QELISELEAELQETRQEM 279
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
442-801 5.80e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 44.27  E-value: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  442 KVIL--MESLCQQSDKLEHFSRqieyfRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLsnt 519
Cdd:TIGR01612  496 KLILmrMKDFKDIIDFMELYKP-----DEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKEL--- 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  520 lkmaEQDNKEAQEMIGALKERSHHMERIIEsEQKGKAALAATLEEyKATVASDQIEMNR----LKAQLENEKQKVAELYS 595
Cdd:TIGR01612  568 ----EEENEDSIHLEKEIKDLFDKYLEIDD-EIIYINKLKLELKE-KIKNISDKNEYIKkaidLKKIIENNNAYIDELAK 641
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  596 IH--------NSGDK--SDIQDLLESV---RLDKEKAEtLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQeeakkqi 662
Cdd:TIGR01612  642 ISpyqvpehlKNKDKiySTIKSELSKIyedDIDALYNE-LSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ------- 713
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  663 edlNMTLEKLRSDLDEKETERSDMKETIFELEDEVeqHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHrRLREE 742
Cdd:TIGR01612  714 ---NMETATVELHLSNIENKKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSK 787
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  743 SAEWRQFQADlqtAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR01612  788 ISEIKNHYND---QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
134-817 6.35e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.88  E-value: 6.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  134 QSKKLPSAGQGANDMALAKRSRSRTATECDVRMS------KSKSDNQISDRAALEAKVKDLLTLAKTKDvEILHLRNELR 207
Cdd:TIGR00606  403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtiELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELR 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  208 DMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK 287
Cdd:TIGR00606  482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  288 LFGYQSLSPeitpgNQSDGGGTLtSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEvyQPLTSSDDALDAPS 367
Cdd:TIGR00606  562 LTSLLGYFP-----NKKQLEDWL-HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--QLSSYEDKLFDVCG 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  368 SSESEG-----IPSIERSRKGSSGNASEVSVacLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENeRLGEEK 442
Cdd:TIGR00606  634 SQDEESdlerlKEEIEKSSKQRAMLAGATAV--YSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL-RLAPDK 710
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  443 VILMESLCQQSDKlehfsrqieyfrslldehhisyvidedvksgrymeleqrymdlaenarfEREQLLGVQQHLSNTLKM 522
Cdd:TIGR00606  711 LKSTESELKKKEK-------------------------------------------------RRDEMLGLAPGRQSIIDL 741
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  523 AEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKaTVASDQIEMNRLKAQLENEKQKVAELYSIHNSGD- 601
Cdd:TIGR00606  742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDl 820
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  602 ----------KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD---AIAKVEDEYRAFQEeakkQIEDLNMT 668
Cdd:TIGR00606  821 drtvqqvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE----QLVELSTE 896
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKH-------------------DME 729
Cdd:TIGR00606  897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqdgkddylkQKE 976
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  730 REIKTLHRRLREESAEWRQFQADLQTavvIANDIKSEAQEE------IGDLKRR--LHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR00606  977 TELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnLTLRKREneLKEVEEELKQHLKEMGQMQVLQMK 1053
                          730
                   ....*....|....*.
gi 2203400754  802 EERGRVYNYMNAVERD 817
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRN 1069
PRK12704 PRK12704
phosphodiesterase; Provisional
616-792 6.56e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 6.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  616 KEKAETLASSLQEDLAHTRNDANR-----LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:PRK12704    26 KKIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  691 FELEDEVEQHRAvklhdnlIISDLENTVKKLqdqkhdmEREIKTLHRRLREESAEWRQFQADLQTAVVIANdIKSEAQEE 770
Cdd:PRK12704   106 EKREEELEKKEK-------ELEQKQQELEKK-------EEELEELIEEQLQELERISGLTAEEAKEILLEK-VEEEARHE 170
                          170       180
                   ....*....|....*....|...
gi 2203400754  771 IGDLKRRLH-EAQEKNEKLTKEL 792
Cdd:PRK12704   171 AAVLIKEIEeEAKEEADKKAKEI 193
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
404-806 6.81e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  404 EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSdklEHFSrQIEYFRSLLdehhisyvidedv 483
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET---ELCA-EAEEMRARL------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  484 kSGRYMELEQRYMDLaeNARFEREQLLGVQQHlsntlkmaeQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAA--- 560
Cdd:pfam01576   67 -AARKQELEEILHEL--ESRLEEEEERSQQLQ---------NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkik 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  561 TLEEYKATVASDQIEMNRLKAQLEN-----------EKQKVAELYSIHNSGDK--SDIQDLL---ESVRLDKEKA----E 620
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEEriseftsnlaeEEEKAKSLSKLKNKHEAmiSDLEERLkkeEKGRQELEKAkrklE 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  621 TLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam01576  215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALarleeetaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  691 FELEDEVEQHRAvKLHDNLiisDLENTVKKLQDQKhdmEREIKTLHRRLREESaewRQFQADLQ-------TAVVIANDI 763
Cdd:pfam01576  295 RDLGEELEALKT-ELEDTL---DTTAAQQELRSKR---EQEVTELKKALEEET---RSHEAQLQemrqkhtQALEELTEQ 364
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2203400754  764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:pfam01576  365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
708-804 7.80e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 7.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  708 NLIISDLENTVKKLQDQKHDME---REIKTLHRRLREESAEWRQ-FQADLQTAVVIANDIKSEAQEEIGDLKRRL----- 778
Cdd:PRK00409   519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2203400754  779 --------HEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PRK00409   599 ggyasvkaHELIEARKRLNKANEKKEKKKKKQKE 632
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
575-957 8.94e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.50  E-value: 8.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  575 EMNRLKAQLENEKQKVAELYS----IHNSGDKSDIQDL--LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:PTZ00108  1003 KLERELARLSNKVRFIKHVINgelvITNAKKKDLVKELkkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL 1082
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  649 DEYRAFQEEAKKQIEDLNMT-LEKLRSDLDEKETERSDMKETifeledEVEQhravklhdnLIISDLENTVKKLQDQKHD 727
Cdd:PTZ00108  1083 GAAVSYDYLLSMPIWSLTKEkVEKLNAELEKKEKELEKLKNT------TPKD---------MWLEDLDKFEEALEEQEEV 1147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  728 MEREIKTlHRRLREesaewRQFQADLQTAVVIANDIKSEAQEEIGDLKRrlhEAQEKNEKLTKELEEIKSRKQEEERGRV 807
Cdd:PTZ00108  1148 EEKEIAK-EQRLKS-----KTKGKASKLRKPKLKKKEKKKKKSSADKSK---KASVVGNSKRVDSDEKRKLDDKPDNKKS 1218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  808 YNYMNAVERDLAALRQGMGLS--RRSSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAvspmqr 885
Cdd:PTZ00108  1219 NSSGSDQEDDEEQKTKPKKSSvkRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRP------ 1292
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  886 HSISGPISTSKPLTALSDKRPNygeipvqEHLLRTSSASRPASLPRVPAMES-AKTLSVSRRSSEEVKRDISA 957
Cdd:PTZ00108  1293 DGESNGGSKPSSPTKKKVKKRL-------EGSLAALKKKKKSEKKTARKKKSkTRVKQASASQSSRLLRRPRK 1358
PRK10884 PRK10884
SH3 domain-containing protein; Provisional
727-784 9.05e-04

SH3 domain-containing protein; Provisional


Pssm-ID: 182809 [Multi-domain]  Cd Length: 206  Bit Score: 41.95  E-value: 9.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400754  727 DMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 784
Cdd:PRK10884    97 DLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNQLIVAQKK 154
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
490-796 1.02e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  490 ELEQRYMDLAEN--ARFErEQLLGVQQhLSNTLKM--AEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAAT 561
Cdd:PRK04778    68 EWRQKWDEIVTNslPDIE-EQLFEAEE-LNDKFRFrkAKHEINEIESLLDLIEEDIEQIleelQELLESEEKNREEVEQL 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  562 LEEY---KATV---------ASDQIEmnrlkAQLENEKQKVAELYSIHNSGDKsdiqdllesvrldkEKAETLASSLQED 629
Cdd:PRK04778   146 KDLYrelRKSLlanrfsfgpALDELE-----KQLENLEEEFSQFVELTESGDY--------------VEAREILDQLEEE 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  630 LAHTRNDANRLQDAIAKVEDEYRAfqeeakkQIEDLNMTLEKLRSD---LDEKetersDMKETIFELEDEVEQHRAvklh 706
Cdd:PRK04778   207 LAALEQIMEEIPELLKELQTELPD-------QLQELKAGYRELVEEgyhLDHL-----DIEKEIQDLKEQIDENLA---- 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  707 dnlIISDLEntVKKLQDQKHDMEREIKTLHRRLREEsaewrqfqadlqtavVIAndiKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:PRK04778   271 ---LLEELD--LDEAEEKNEEIQERIDQLYDILERE---------------VKA---RKYVEKNSDTLPDFLEHAKEQNK 327
                          330
                   ....*....|
gi 2203400754  787 KLTKELEEIK 796
Cdd:PRK04778   328 ELKEEIDRVK 337
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
398-804 1.10e-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: 43.17  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHSTSEELQATLQE----LADLQQITQELNSENERLG---EEKVILMESLCQQSDKLEHFSRQIEYFRSLL 470
Cdd:pfam05483   88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKVSlklEEEIQENKDLIKENNATRHLCNLLKETCARS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  471 DEHHISYVIDEDVKSGRYMELEQRYMDL----------AENARFEREQLLGVQ----QHLSNTLKmAEQDNKEaqemiga 536
Cdd:pfam05483  168 AEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqAENARLEMHFKLKEDhekiQHLEEEYK-KEINDKE------- 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  537 lKERSHHMERIIESEQKGKAaLAATLEEYKATV----ASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS--------- 603
Cdd:pfam05483  240 -KQVSLLLIQITEKENKMKD-LTFLLEESRDKAnqleEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalee 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  604 DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE-- 678
Cdd:pfam05483  318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEmt 397
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  679 -----KETERSDMKETIFELEDEVEQHRAV-KLHDNLIISDLENT--VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQ 750
Cdd:pfam05483  398 kfknnKEVELEELKKILAEDEKLLDEKKQFeKIAEELKGKEQELIflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2203400754  751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05483  478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
PHA03247 PHA03247
large tegument protein UL36; Provisional
828-967 1.12e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  828 SRRSSTSSEPTPTVKTLIKSF----DSASQVPNPAAAAIPRT----PLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLT 899
Cdd:PHA03247  2878 PARPPVRRLARPAVSRSTESFalppDQPERPPQPQAPPPPQPqpqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400754  900 ALSDKRPNY---GEIPVQEHLLRTSSASRPASLPRVPameSAKTLSVSRRSSEEVKRDISAQEGASPASLM 967
Cdd:PHA03247  2958 AVPQPWLGAlvpGRVAVPRFRVPQPAPSREAPASSTP---PLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
516-799 1.15e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  516 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVaelys 595
Cdd:TIGR04523  396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL----- 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  596 ihnsgdkSDIQDLLESVRLDKEKaetlassLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSD 675
Cdd:TIGR04523  471 -------KVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  676 LDEKETERSDMKETIFELEDeveqhravklhdnliisdlENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQT 755
Cdd:TIGR04523  533 KKEKESKISDLEDELNKDDF-------------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2203400754  756 AVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:TIGR04523  594 KEKEKKDLIKEIEEkekKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
607-823 1.24e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  607 DLLESVRLDKEKAETLASSLQEDLAHTR-------------NDANRLQDAIAKVEDEYRAFQ-----EEAKKQIEDLNMT 668
Cdd:COG3206    104 NLDEDPLGEEASREAAIERLRKNLTVEPvkgsnvieisytsPDPELAAAVANALAEAYLEQNlelrrEEARKALEFLEEQ 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  669 LEKLRSDLDEKETERSDMKET--IFELEDEVEQHRAvklhdnlIISDLENTVKKLQDQKhdmeREIKTLHRRLREESAEW 746
Cdd:COG3206    184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQ-------QLSELESQLAEARAEL----AEAEARLAALRAQLGSG 252
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  747 RQFQADLQTAVVIANDIK--SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvyNYMNAVERDLAALRQ 823
Cdd:COG3206    253 PDALPELLQSPVIQQLRAqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----RILASLEAELEALQA 327
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
404-794 1.34e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  404 EENQH--STSEELQATLQELADLQQITQELNSENERLGEEKVILM----ESLCQQSDKLEHFSRQIEYFRSLLDEhhisy 477
Cdd:pfam10174   67 EENQHlqLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelteENFRRLQSEHERQAKELFLLRKTLEE----- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  478 videdvksgryMELEQRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGAlKERSHHMERIIESEQKGKA 556
Cdd:pfam10174  142 -----------MELRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIAEA-EMQLGHLEVLLDQKEKENI 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  557 ALAATLeEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDL------ 630
Cdd:pfam10174  210 HLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSL--------ERNIRDLEDEVQMLKTNGLLHTEDREEEIkqmevy 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  631 -AHT---RNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTL--------------EKLRSDLDEKETE 682
Cdd:pfam10174  281 kSHSkfmKNKIDQLKQELSKKESELLALQtkletltnqnSDCKQHIEVLKESLtakeqraailqtevDALRLRLEEKESF 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  683 RSDMKETIFELEDE--VEQHRAVKLHDNLIISD-----LENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQAD 752
Cdd:pfam10174  361 LNKKTKQLQDLTEEksTLAGEIRDLKDMLDVKErkinvLQKKIENLQEQLRDKDKQLAGLKERvksLQTDSSNTDTALTT 440
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  753 LQTAVVIANDI-----------KSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:pfam10174  441 LEEALSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSALQPELTE 493
mukB PRK04863
chromosome partition protein MukB;
398-665 1.37e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  398 ERIHQMEENQHSTSEELQATLQEL-ADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHfSRQIEYFRSLL 470
Cdd:PRK04863   424 ERAKQLCGLPDLTADNAEDWLEEFqAKEQEATEELLSLEQKLSVAQAAHsqfeqaYQLVRKIAGEVSR-SEAWDVARELL 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  471 DEHhisyvidedvksgrymeleqrymdlaENARFEREQLLGVQQHLSnTLKMAEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:PRK04863   503 RRL--------------------------REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  551 EQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSI----HNSgdksdiQDLLEsvRLDKEKAETLASSl 626
Cdd:PRK04863   556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawLAA------QDALA--RLREQSGEEFEDS- 626
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2203400754  627 qEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDL 665
Cdd:PRK04863   627 -QDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
412-808 1.54e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.42  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKs 485
Cdd:pfam05557  156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskseLARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLK- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  486 gRYMELEQRYMDLAENARFEREQLLG--------VQQH---------LSNTLKMAEQDNKEAQEMIGALKERSHHMERII 548
Cdd:pfam05557  235 -RKLEREEKYREEAATLELEKEKLEQelqswvklAQDTglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  549 -ESEQKGKAALAATLEEYKATVASDQI-------------EMNRLKAQLEN-EKQKVAELYSIHNSGDKSDIQDLLESVR 613
Cdd:pfam05557  314 rELEQELAQYLKKIEDLNKKLKRHKALvrrlqrrvllltkERDGYRAILESyDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEdeyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFEL 693
Cdd:pfam05557  394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  694 EDEVEQH-----------RAVKLHDNliisdleNTVKKLQDQKHDMER---EIKTLHRRLreesaewRQFQADLQTAVVI 759
Cdd:pfam05557  468 EMELERRclqgdydpkktKVLHLSMN-------PAAEAYQQRKNQLEKlqaEIERLKRLL-------KKLEDDLEQVLRL 533
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2203400754  760 ANDIKSEAQEEIGDLKRRLHEAQEKNEKltkeLEEIKSRKQEEERGRVY 808
Cdd:pfam05557  534 PETTSTMNFKEVLDLRKELESAELKNQR----LKEVFQAKIQEFRDVCY 578
PRK01156 PRK01156
chromosome segregation protein; Provisional
412-813 1.94e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI---------SYVIDED 482
Cdd:PRK01156   190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyeseiktaeSDLSMEL 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  483 VKSGRYMELEQRYMDLAENARF-EREQLLGVQqhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKaalaat 561
Cdd:PRK01156   270 EKNNYYKELEERHMKIINDPVYkNRNYINDYF-----KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY------ 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  562 leeykatvaSDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAnrlq 641
Cdd:PRK01156   339 ---------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAFISEILKIQEIDP---- 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  642 DAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETE------RSDMKETIFELEDEVEQHravklhdnlIISDLE 715
Cdd:PRK01156   405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNmemlngQSVCPVCGTTLGEEKSNH---------IINHYN 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  716 NTVKKLQDQKHDMEREIKTLHRRLRE-ESAEWRQFQADLQTAVVIANDIKSeAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:PRK01156   476 EKKSRLEEKIREIEIEVKDIDEKIVDlKKRKEYLESEEINKSINEYNKIES-ARADLEDIKIKINELKDKHDKYEEIKNR 554
                          410
                   ....*....|....*....
gi 2203400754  795 IKSRKQEEERGRVYNYMNA 813
Cdd:PRK01156   555 YKSLKLEDLDSKRTSWLNA 573
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
544-864 1.97e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  544 MERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdiQDLLESVRLDKEKAETLA 623
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL------------EEELEELNEQLQAAQAEL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  624 SSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqiedLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV 703
Cdd:COG4372     97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ----LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  704 KLhdNLIISDLENTVKKLQDQ---------KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDL 774
Cdd:COG4372    173 LQ--ALSEAEAEQALDELLKEanrnaekeeELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  775 KRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQV 854
Cdd:COG4372    251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
                          330
                   ....*....|
gi 2203400754  855 PNPAAAAIPR 864
Cdd:COG4372    331 ALAILLAELA 340
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
1017-1094 2.37e-03

second 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, and are probably involved in the 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409145  Cd Length: 109  Bit Score: 38.65  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754 1017 LLKWC--QKKTEGYQNIdITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMV 1094
Cdd:cd21296     15 LLKWMnfHLKKAGYKKT-VTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEKMNCKRYLTAKDIV 93
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
419-778 2.79e-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: 41.88  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  419 QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhisyvideDVKSGRYMELEQRYMDL 498
Cdd:TIGR00618  542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV----------RLQDLTEKLSEAEDMLA 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  499 AENarfeREQLLGVQQHLSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQiemnR 578
Cdd:TIGR00618  612 CEQ----HALLRKLQPEQDLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ----L 680
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  579 LKAQLENEKQKVA---ELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQE------DLAHTRNDANRLQDAI--AKV 647
Cdd:TIGR00618  681 ALQKMQSEKEQLTywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDlaaredALNQSLKELMHQARTVlkART 760
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  648 EDEYRAFQEEAkkQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR-----AVKLHDNLIISDLENTVKKLQ 722
Cdd:TIGR00618  761 EAHFNNNEEVT--AALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdedILNLQCETLVQEEEQFLSRLE 838
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400754  723 dQKHDMEREIKTLHRRLREES---AEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRL 778
Cdd:TIGR00618  839 -EKSATLGEITHQLLKYEECSkqlAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKF 896
mukB PRK04863
chromosome partition protein MukB;
495-801 2.81e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  495 YMDLAENARFEREQLLGVQQHLSN---TLKMAEQDNKEAQEMIGALKERSHHMERIIESeQKGKAALAATLEEYKATVAS 571
Cdd:PRK04863   274 YMRHANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIER 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  572 DQIEMNRLKAQLENEKQKVAElysihnsgdksdIQDLLESVRLDKEKAET----LASSL---QE--DLAHTR----NDAN 638
Cdd:PRK04863   353 YQADLEELEERLEEQNEVVEE------------ADEQQEENEARAEAAEEevdeLKSQLadyQQalDVQQTRaiqyQQAV 420
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  639 RLQD-----------AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEK---------------ETERSDMKETIFE 692
Cdd:PRK04863   421 QALErakqlcglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvrkiagEVSRSEAWDVARE 500
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  693 LEDEVEQHRAvklhdnliisdlentvkkLQDQKHDMEREIKTLHRRLREESAEWR-------QFQADLQTAVViANDIKS 765
Cdd:PRK04863   501 LLRRLREQRH------------------LAEQLQQLRMRLSELEQRLRQQQRAERllaefckRLGKNLDDEDE-LEQLQE 561
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2203400754  766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:PRK04863   562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
508-806 2.93e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  508 QLLGVQQHLSNTLKMAEQDN--KEAQEMIGALKE-RSHHMERIIESEQKGKAALAATleEYKATVASDQ----IEMNRLK 580
Cdd:pfam17380  273 QLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQermaMEREREL 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  581 AQLENEKQKvAELYSIHNSGDKSDIQDLLESVRLDKEKAEtlasslqedlahtRNDANRLQDAIAKvedEYRAFQEEAKK 660
Cdd:pfam17380  351 ERIRQEERK-RELERIRQEEIAMEISRMRELERLQMERQQ-------------KNERVRQELEAAR---KVKILEEERQR 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  661 QIEDLNMTLEKLRSDldEKETERSDMKETIFELEDEVEQHRAVKLhdnliisDLENTVKKLQDQKHDMEReiktlhRRLR 740
Cdd:pfam17380  414 KIQQQKVEMEQIRAE--QEEARQREVRRLEEERAREMERVRLEEQ-------ERQQQVERLRQQEEERKR------KKLE 478
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400754  741 EESAEWRQFQADLQTAVVIandikseaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:pfam17380  479 LEKEKRDRKRAEEQRRKIL--------EKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR 536
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
555-825 3.35e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  555 KAALAATLEEYKATVASDQ----IEMNRLKAQLENEK-QKVAELYSihnsgdksDIQDLLESVRLDKEKAETLAS----- 624
Cdd:PRK05771     8 KVLIVTLKSYKDEVLEALHelgvVHIEDLKEELSNERlRKLRSLLT--------KLSEALDKLRSYLPKLNPLREekkkv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  625 ---SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEaKKQIEDLNMTLEKLRS-DLDEKETERSDMKETIF-----ELED 695
Cdd:PRK05771    80 svkSLEELIKDVEEELEKIEKEIKELEEEISELENE-IKELEQEIERLEPWGNfDLDLSLLLGFKYVSVFVgtvpeDKLE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  696 EVEQhrAVKLHDNLIISDLENT----VKKLQDQKHDMEREIKTLhrrlreesaEWRQFQAdlqtavviaNDIKSeAQEEI 771
Cdd:PRK05771   159 ELKL--ESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKL---------GFERLEL---------EEEGT-PSELI 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2203400754  772 GDLKRRLHEAQEKNEKLTKELEEIKsRKQEEERGRVYNYM-NAVERDLAALRQGM 825
Cdd:PRK05771   218 REIKEELEEIEKERESLLEELKELA-KKYLEELLALYEYLeIELERAEALSKFLK 271
PRK11637 PRK11637
AmiB activator; Provisional
539-659 3.36e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  539 ERSHHMERII-------ESEQKGKAALAATLEEykatvasdqieMNRLKAQLENEKQKVAELYSihnsgDKSDIQDLLES 611
Cdd:PRK11637   149 EESQRGERILayfgylnQARQETIAELKQTREE-----------LAAQKAELEEKQSQQKTLLY-----EQQAQQQKLEQ 212
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  612 VRLDKEKAET-LASSLQED---LAHTRNDANRLQDAIAKVEDEYRAFQE-EAK 659
Cdd:PRK11637   213 ARNERKKTLTgLESSLQKDqqqLSELRANESRLRDSIARAEREAKARAErEAR 265
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
396-592 3.83e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG4942     32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE--- 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  476 syVIDEDVKSGRYMELE--------------QRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKER 540
Cdd:COG4942    109 --LLRALYRLGRQPPLAlllspedfldavrrLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEE 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2203400754  541 SHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:COG4942    187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
660-754 3.84e-03

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 37.97  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDeVEQHRAV--KLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:pfam01920    2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELEL-LDEDTKVykLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
                           90
                   ....*....|....*..
gi 2203400754  738 RLREESAEWRQFQADLQ 754
Cdd:pfam01920   81 QLEKLEKELEELKEELY 97
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
656-810 3.99e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  656 EEAKKQIEDLNMTLEKLRSDLDEKETErsdMKETIFELEDEVEQhrAVKLHDNL--IISDLENTVKKLqdqKHDMEREIK 733
Cdd:PRK00409   505 EEAKKLIGEDKEKLNELIASLEELERE---LEQKAEEAEALLKE--AEKLKEELeeKKEKLQEEEDKL---LEEAEKEAQ 576
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  734 TLHRRLREESAEWRQFQADLQTAVVIAndIKSEAQEEIgdlKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNY 810
Cdd:PRK00409   577 QAIKEAKKEADEIIKELRQLQKGGYAS--VKAHELIEA---RKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSL 648
46 PHA02562
endonuclease subunit; Provisional
507-736 4.80e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMEriIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:PHA02562   195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEeaKTIKAE--IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  585 NeKQKVAELYSIHN-----SGDKSDIQDLLESVrldKEKAETLASSLqedlahtrNDANRLQDAIAKVEDEYRafqeEAK 659
Cdd:PHA02562   273 Q-FQKVIKMYEKGGvcptcTQQISEGPDRITKI---KDKLKELQHSL--------EKLDTAIDELEEIMDEFN----EQS 336
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400754  660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKTLH 736
Cdd:PHA02562   337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE-------LAKLQDELDKIVKTKSELVKEKYHRG 406
PTZ00121 PTZ00121
MAEBL; Provisional
520-804 4.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  520 LKMAEQDNKEAQEMIGAlkERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS 599
Cdd:PTZ00121  1502 AKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  600 GDKSDiqdllESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAfqEEAKKQIEDLNMTL--EKLRSDLD 677
Cdd:PTZ00121  1580 LRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEaeEKKKAEEL 1652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  678 EKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDME--REIKTLHRRLREESAEWRQFQADLQT 755
Cdd:PTZ00121  1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEE 1727
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2203400754  756 AVVIANDIKSEAQEEigdlKRRLHEAQ--EKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121  1728 NKIKAEEAKKEAEED----KKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIR 1774
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
516-802 5.98e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  516 LSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQkgkaalaatleEYKATVASDQIEMNRLKAQLENEKQKVAELYS 595
Cdd:TIGR04523  347 LKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  596 -IHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFqeeaKKQIEDLNMTLEKLR 673
Cdd:TIGR04523  413 qIKKlQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQ 488
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  674 SDLDEKETERSDMKETIFELEDEVeqhraVKLHDNliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADl 753
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKV-----KDLTKK--ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE- 560
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2203400754  754 qtavvianDIKSEAQEEIgdlkRRLHEAQEKNEKLTKELEEIKSRKQEE 802
Cdd:TIGR04523  561 --------KEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKE 597
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
412-673 6.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  412 EELQATLQELADLQQITQELNSENERLgeekvilmeslcqqSDKLEHFSRQIEYFRSLLDehhISYVIDEdvksgrYMEL 491
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDAL--------------QERREALQRLAEYSWDEID---VASAERE------IAEL 673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  492 EQRYMDL-AENARFE--REQLLGVQQhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIES--------EQKGKAALAA 560
Cdd:COG4913    674 EAELERLdASSDDLAalEEQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaEDLARLELRA 749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  561 TLEEYKATVASDQIE----------MNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESV--------RLDKEKAETL 622
Cdd:COG4913    750 LLEERFAAALGDAVErelrenleerIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpeylaLLDRLEEDGL 829
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2203400754  623 AsSLQEDLAHTRNDA--NRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLR 673
Cdd:COG4913    830 P-EYEERFKELLNENsiEFVADLLSKLRRA----IREIKERIDPLNDSLKRIP 877
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
407-673 8.88e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 8.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  407 QHSTSEELQATLQELAD------LQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQieyfrslldehHISYVID 480
Cdd:COG3206    143 TSPDPELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-----------NGLVDLS 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  481 EDVKS--GRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQE--MIGALKERshhmeriieseqkgKA 556
Cdd:COG3206    212 EEAKLllQQLSELESQL----AEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQ--------------LA 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400754  557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRND 636
Cdd:COG3206    274 ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE-----------AQRILASLEAELEALQAREASLQAQLAQLEAR 342
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2203400754  637 ANRLqdaiAKVEDEYRAFQEEAKKQIEDLNMTLEKLR 673
Cdd:COG3206    343 LAEL----PELEAELRRLEREVEVARELYESLLQRLE 375
 
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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