|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.64e-110 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 349.96 E-value: 2.64e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 35 CYPATGDLLIGRaqKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHetlnpdSHLIENVVTTFAPNRLKiWWQS 114
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 115 ENGV---ENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFpGISTGPMK--KVDDII 189
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 190 CDSRYSDIEPSTEGEVIFRAL--DPAFKIEDpYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIReKYYYAVYDMVV 267
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 1666305206 268 RG 269
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
8.77e-85 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 277.32 E-value: 8.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 29 GCAEGSCYPATGDLLIGRaqKLSVTSTCGLHKPEPYCI-VSHLQEDKKCFICDSRDPYHetlnpdSHLIENVVTTFAPNR 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 108 LKiWWQSEN---GVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSsDFGKAWGVYRYFAYDCESSFPGISTGPMKK 184
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 185 V--DDIICDSRYSDIEPSTEGEVIFRALDPAFKIED-PYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYA 261
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 1666305206 262 VYDMVVRG 269
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1714-1786 |
2.22e-38 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 137.99 E-value: 2.22e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1714 DARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL 1786
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTCL 73
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1456-1776 |
6.49e-20 |
|
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: 97.43 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSeaKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNL---IKQIRNFLTEDSADLDSIE----AVANEV 1528
Cdd:TIGR02168 220 AELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQkelyALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 LKMEmpstpQQLQNLTEDIRERVETLSQVEVILQQSAAdiaRAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVA 1608
Cdd:TIGR02168 298 SRLE-----QQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1609 AEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEyiEKVVYSVKQNADDVKK 1688
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1689 tldgELDEKYKKVESLIAQKtEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEV 1768
Cdd:TIGR02168 448 ----ELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
|
....*...
gi 1666305206 1769 RSLLKDIS 1776
Cdd:TIGR02168 523 GVLSELIS 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1457-1778 |
2.22e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1457 EVEQLSKMVSEAKvRADEAKQNAQDVLLKTNATKEKVDKSNEdlrnlikqirnfltEDSADLDSIEAVANEVLKMEMPST 1536
Cdd:PTZ00121 1303 KADEAKKKAEEAK-KADEAKKKAEEAKKKADAAKKKAEEAKK--------------AAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1537 PQQLQnlTEDIRERVETLsqvevilQQSAADIARAEllleEAKrasKSATDVKVTADMVKEALEEAEKAQVAAEKA--IK 1614
Cdd:PTZ00121 1368 AAEKK--KEEAKKKADAA-------KKKAEEKKKAD----EAK---KKAEEDKKKADELKKAAAAKKKADEAKKKAeeKK 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1615 QADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKaAQNSGEAEYIEKVVYSVKQNADDVKKTLDGEL 1694
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1695 D-EKYKKVESliAQKTEES--ADARRKAELLQNEAKTLLAQANSKLQLLEDLE--RKYEDNQKYLEDKAQELVRLEgevr 1769
Cdd:PTZ00121 1511 KaDEAKKAEE--AKKADEAkkAEEAKKADEAKKAEEKKKADELKKAEELKKAEekKKAEEAKKAEEDKNMALRKAE---- 1584
|
....*....
gi 1666305206 1770 sLLKDISEK 1778
Cdd:PTZ00121 1585 -EAKKAEEA 1592
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
773-818 |
1.28e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 72.34 E-value: 1.28e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGC 818
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
821-869 |
1.63e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.00 E-value: 1.63e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 821 CDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPSCQPCQC 869
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1778 |
3.57e-15 |
|
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: 79.42 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1559 VILQQSAADIARAELLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAEL----------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1639 ETLTNASQRISKLERNVEELKRK------AAQNSGEAEYIE------------KVVYSVKQNADDVKKTLDgELDEKYKK 1700
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaellrALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1701 VESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
773-821 |
7.90e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 70.07 E-value: 7.90e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPC 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-819 |
1.12e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.12e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 772 ACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGF--GPNGCK 819
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1251-1773 |
2.32e-12 |
|
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: 72.52 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEA-------EKLTKDvtEKMAQVEVKLTDTASQSNStagelgaLQAEAESLDKTVKE----LAEQLEFIKN-------- 1311
Cdd:pfam01576 115 EEAarqklqlEKVTTE--AKIKKLEEDILLLEDQNSK-------LSKERKLLEERISEftsnLAEEEEKAKSlsklknkh 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1312 ----SDIQGALDSITKYFQmSLEAEKR-VNASTTDPNstvEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQ 1386
Cdd:pfam01576 186 eamiSDLEERLKKEEKGRQ-ELEKAKRkLEGESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1387 SLdlSAVAQMTCGTPPGADCSESECGGPN----CRTDEGEKKCGGPGCGgLVTVAHSAWQKAMDFDRDvlsalAEVEQLS 1462
Cdd:pfam01576 262 AL--KKIRELEAQISELQEDLESERAARNkaekQRRDLGEELEALKTEL-EDTLDTTAAQQELRSKRE-----QEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1463 KMVSEaKVRADEAKqnAQDVLLKTNATkekVDKSNEDLRNLiKQIRNFLTEDSADLDSieavANEVLKMEMpSTPQQLQN 1542
Cdd:pfam01576 334 KALEE-ETRSHEAQ--LQEMRQKHTQA---LEELTEQLEQA-KRNKANLEKAKQALES----ENAELQAEL-RTLQQAKQ 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1543 LTEDIRERVEtlSQV-EVILQQSAADIARAELlleeAKRASKSATDVkvtaDMVKEALEEAEKAQVAAEKAIKQADEDIQ 1621
Cdd:pfam01576 402 DSEHKRKKLE--GQLqELQARLSESERQRAEL----AEKLSKLQSEL----ESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1622 GTQNLLtsiesetaaSEETLT--NASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELdekyK 1699
Cdd:pfam01576 472 DTQELL---------QEETRQklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA----G 538
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1700 KVESLiaqktEEsadARRKaelLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLK 1773
Cdd:pfam01576 539 TLEAL-----EE---GKKR---LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
3.63e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.63e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRAC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
820-863 |
7.75e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 7.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 820 PCDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPS 863
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1132-1171 |
8.67e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 8.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1666305206 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSG 1171
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
821-864 |
4.29e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.29e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 821 CDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWG--FPSC 864
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1132-1176 |
4.92e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.92e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGV-FPDC 1176
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1131-1180 |
7.20e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 7.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1131 ACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCH 1180
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1126 |
8.84e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 8.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 1083 PCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPD 1126
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1129 |
3.83e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.83e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVEC 1129
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-508 |
4.06e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 4.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1666305206 457 SCACNPLGTIPGGnpCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCR 508
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1028-1082 |
4.25e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1028 CVCNYLGTVKEHCngsdchcDKATGQCSCLPNVIGQNCDRCAPNTWQLASGTGCG 1082
Cdd:pfam00053 1 CDCNPHGSLSDTC-------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1188-1675 |
4.33e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1188 AIIGELTNRTHKflEKAKALKISGVIGP-YRETVDSVEKKVNEIKDILAQ-SPAAEPLKNIGILFEEAEKLTKDVTEKMA 1265
Cdd:COG4717 42 FIRAMLLERLEK--EADELFKPQGRKPElNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1266 QVEVKLtdtasQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKN--SDIQGALDSITKYFQmSLEAEKRVNASTTDpn 1343
Cdd:COG4717 120 KLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELREleEELEELEAELAELQE-ELEELLEQLSLATE-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1344 STVEQSALTRDRVEDLMLERESPFKEQQEEQARL---LDELAGKLQSLDLSAVAQMTCGTPPGAdcSESECGGPNCRTDE 1420
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELEAAALEERLKEARLLLLIA--AALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1421 GEKKCGGPGCGGLVTVAHSAWQKamdFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVD---KSN 1497
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLL---LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLellDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1498 EDLRNLIKQIRNflTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQsaadiaraellLEE 1577
Cdd:COG4717 347 EELQELLREAEE--LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-----------LEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1578 AKRASKSATDvKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLtsiesETAASEETLTNASQRISKLERNVEE 1657
Cdd:COG4717 414 LLGELEELLE-ALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQELEELKAELRE 487
|
490
....*....|....*...
gi 1666305206 1658 LKRKAAQNSGEAEYIEKV 1675
Cdd:COG4717 488 LAEEWAALKLALELLEEA 505
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-512 |
4.82e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.82e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 458 CACNPLGTIPGGnpCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLdgcrPCDC 512
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-455 |
5.06e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 5.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 398 CTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLSAEDPYGC 455
Cdd:pfam00053 1 CDCNPHGSLSDT-CDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1456-1691 |
1.31e-09 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 60.76 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNF-----LTEDSAD------LD-SIEA 1523
Cdd:smart00283 39 ANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIgeivsVIDDIADqtnllaLNaAIEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 ------------VANEVlkmempstpqqlQNLTEdirervETlsqvevilQQSAADIarAELLLEEAKRASKSATDVKVT 1591
Cdd:smart00283 119 arageagrgfavVADEV------------RKLAE------RS--------AESAKEI--ESLIKEIQEETNEAVAAMEES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 ADMVKEALEEAEKAqvaaekaiKQADEDI-QGTQNLLTSIESETAASEETlTNASQRISkleRNVEELKRKAAQNSGEAE 1670
Cdd:smart00283 171 SSEVEEGVELVEET--------GDALEEIvDSVEEIADLVQEIAAATDEQ-AAGSEEVN---AAIDEIAQVTQETAAMSE 238
|
250 260
....*....|....*....|.
gi 1666305206 1671 YIEKVVYSVKQNADDVKKTLD 1691
Cdd:smart00283 239 EISAAAEELSGLAEELDELVE 259
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1217-1770 |
2.17e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1217 RETVDSVEKKVNEIKDILAQSPA-AEPLKNIGIlfEEAEKLTKDVTEKMAQVEVKLTDTASQsnsTAGELGALQAEAESL 1295
Cdd:NF041483 469 REAVQQIEEAARTAEELLTKAKAdADELRSTAT--AESERVRTEAIERATTLRRQAEETLER---TRAEAERLRAEAEEQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1296 DKTVKELAEQLEFIKNSDIQGAL-----DSITKYFQMSLEAEKRVNASttdpnstveQSALTRDRVEDLMLERESpfkeq 1370
Cdd:NF041483 544 AEEVRAAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLTAA---------EEALADARAEAERIRREA----- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1371 QEEQARLLDELAGKLQSLDLSAVAQMT-CGTPPGADCSESECGGPNC----RTD---EGEkkcggpgcgGLVTVAhsawQ 1442
Cdd:NF041483 610 AEETERLRTEAAERIRTLQAQAEQEAErLRTEAAADASAARAEGENVavrlRSEaaaEAE---------RLKSEA----Q 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1443 KAMDFDRDVLSALAE--VEQLSKMVSEAKVRADEAKQNAQDVL--LKTNATKEKvDKSNEDLRNLIKQIRNFLTEDSADL 1518
Cdd:NF041483 677 ESADRVRAEAAAAAErvGTEAAEALAAAQEEAARRRREAEETLgsARAEADQER-ERAREQSEELLASARKRVEEAQAEA 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1519 DSIEAVANEvLKMEMPSTPQQlqnLTEDIRERVETL---SQVEVILQQSAADIArAELLLEEAK---------------R 1580
Cdd:NF041483 756 QRLVEEADR-RATELVSAAEQ---TAQQVRDSVAGLqeqAEEEIAGLRSAAEHA-AERTRTEAQeeadrvrsdayaereR 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 ASKSATDVKvtadmvKEALEEAEKAQVAAEKAIKQADEDIQgtqnLLTSIESETAasEETLTNASQRISKLERNV----- 1655
Cdd:NF041483 831 ASEDANRLR------REAQEETEAAKALAERTVSEAIAEAE----RLRSDASEYA--QRVRTEASDTLASAEQDAartra 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 ---EELKRKAAQNSGEAE-YIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEES----ADARRKAELLQNEAK 1727
Cdd:NF041483 899 darEDANRIRSDAAAQADrLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAeqliAEATGEAERLRAEAA 978
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1666305206 1728 TLLAQANsklqllEDLERKYEDNQKYLEDKAQELVRLEGEVRS 1770
Cdd:NF041483 979 ETVGSAQ------QHAERIRTEAERVKAEAAAEAERLRTEARE 1015
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
509-548 |
4.56e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1666305206 509 PCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
866-911 |
4.74e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 866 PCQCNGHA---LDCDTVTGECLsCQDYTTGHNCERCLAGYYGDPIIGSG 911
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1763 |
4.92e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.77 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDlrnlikQIRNFLTEDSA-DLDSIEAVANEVLKM---EMP 1534
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE------KARTVAAEDTAaQLAKAARTAEEVLTKaseDAK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1535 STPQQLQNLTEDIRERVETLSQVeviLQQSAADIA--------------RAEL--LLEEAKRASKSATDVKVtadmvkEA 1598
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADR---LRGEAADQAeqlkgaakddtkeyRAKTveLQEEARRLRGEAEQLRA------EA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1599 LEEAEKAQVAAEK-AIKQADEDIQGTQNLLTSIESE--------TAASEETLTNASQRISKLERNVEE-LKR---KAAQN 1665
Cdd:NF041483 457 VAEGERIRGEARReAVQQIEEAARTAEELLTKAKADadelrstaTAESERVRTEAIERATTLRRQAEEtLERtraEAERL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1666 SGEAEyiekvvysvkQNADDVKKTLDGELDEKYKKVESLIAQKTEESADarrkaEL--LQNEAKTLLAQANSKL----QL 1739
Cdd:NF041483 537 RAEAE----------EQAEEVRAAAERAARELREETERAIAARQAEAAE-----ELtrLHTEAEERLTAAEEALadarAE 601
|
330 340
....*....|....*....|....
gi 1666305206 1740 LEDLERKYEDNQKYLEDKAQELVR 1763
Cdd:NF041483 602 AERIRREAAEETERLRTEAAERIR 625
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
867-914 |
7.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 867 CQCNGHA---LDCDTVTGECLsCQDYTTGHNCERCLAGYYGDPiIGSGDHC 914
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
510-548 |
9.68e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 9.68e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1666305206 510 CDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1028-1081 |
9.87e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 9.87e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1028 CVCNYLGTVkehcngsDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQLAS-GTGC 1081
Cdd:cd00055 2 CDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1028-1081 |
1.02e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1028 CVCNYLGTVkehcngsDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQlASGTGC 1081
Cdd:smart00180 1 CDCDPGGSA-------SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-501 |
1.46e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 458 CACNPLGTIpgGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLS 501
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1251-1755 |
2.05e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.45 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVtekMAQVEvKLTDTASQSNSTAG-ELGALQAEAEsldKTVKELAEQLEFIKnSDiqgaldsitkyfqmSL 1329
Cdd:NF041483 815 EEADRVRSDA---YAERE-RASEDANRLRREAQeETEAAKALAE---RTVSEAIAEAERLR-SD--------------AS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1330 EAEKRVNASTTDPNSTVEQSAlTRDRVEdlmlerespfkeQQEEQARLLDELAGKLQSLdlsaVAQMTcgtppgadcSES 1409
Cdd:NF041483 873 EYAQRVRTEASDTLASAEQDA-ARTRAD------------AREDANRIRSDAAAQADRL----IGEAT---------SEA 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1410 ECGGPNCRTdEGEKKCGGPGCGGLVTVAHSAWQKamdfDRDVLSALAEVEQLSkmvSEAKVRADEAKQNAQDVLLKTNAT 1489
Cdd:NF041483 927 ERLTAEARA-EAERLRDEARAEAERVRADAAAQA----EQLIAEATGEAERLR---AEAAETVGSAQQHAERIRTEAERV 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KEKVDKSNEDLRNLIKqirnflTEDSADLDSIEAVANevlkmempstpqqlqnltediRERVETLSQVEVILQQSAADia 1569
Cdd:NF041483 999 KAEAAAEAERLRTEAR------EEADRTLDEARKDAN---------------------KRRSEAAEQADTLITEAAAE-- 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 rAELLLEEAK-RASKSATDVKVTAD-MVKEALEEAEKAQVAA--------EKAIKQADEDIQGTQNLLTSIESETaasEE 1639
Cdd:NF041483 1050 -ADQLTAKAQeEALRTTTEAEAQADtMVGAARKEAERIVAEAtvegnslvEKARTDADELLVGARRDATAIRERA---EE 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1640 TLTnasqrisKLERNVEELKRKAAQNSGEA-----EYIEKVVYSVKQN---ADDVKKTLDGELDEK--------YKKVES 1703
Cdd:NF041483 1126 LRD-------RITGEIEELHERARRESAEQmksagERCDALVKAAEEQlaeAEAKAKELVSDANSEaskvriaaVKKAEG 1198
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1704 LIAQKTEESADARRKAELLQN----EAKTLLAQANSKLQLL----EDLERKYEDNQKYLE 1755
Cdd:NF041483 1199 LLKEAEQKKAELVREAEKIKAeaeaEAKRTVEEGKRELDVLvrrrEDINAEISRVQDVLE 1258
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-456 |
4.21e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 4.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 397 PCTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLsAEDPYGCK 456
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGT--------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1251-1771 |
4.77e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVTEKM----AQVEV---KLTDTASQSNSTAgelgalQAEAESLDKTVK-ELAEQLEFIKnSDIQGALDSIT 1322
Cdd:NF041483 611 EETERLRTEAAERIrtlqAQAEQeaeRLRTEAAADASAA------RAEGENVAVRLRsEAAAEAERLK-SEAQESADRVR 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1323 KYFQMSLEaekRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLldelagklQSLDLSAVAQMtcgtpp 1402
Cdd:NF041483 684 AEAAAAAE---RVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERARE--------QSEELLASARK------ 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1403 gadcsesecggpncRTDEGEKKCG------GPGCGGLVTVAHSAWQKAmdfdRDVLSALAEV--EQLSKMVSEAKVRADE 1474
Cdd:NF041483 747 --------------RVEEAQAEAQrlveeaDRRATELVSAAEQTAQQV----RDSVAGLQEQaeEEIAGLRSAAEHAAER 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1475 AKQNAQDVL--LKTNATKEKvDKSNEDLRnlikQIRNFLTEDS------ADLDSIEAVAN-EVLKMEMPSTPQQLQNLTE 1545
Cdd:NF041483 809 TRTEAQEEAdrVRSDAYAER-ERASEDAN----RLRREAQEETeaakalAERTVSEAIAEaERLRSDASEYAQRVRTEAS 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1546 DI--------------------RERVETLSQVEVILQQSAADIAR--------AELLLEEA-KRASKSATDVKVTAD-MV 1595
Cdd:NF041483 884 DTlasaeqdaartradaredanRIRSDAAAQADRLIGEATSEAERltaearaeAERLRDEArAEAERVRADAAAQAEqLI 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1596 KEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQriSKLERNVEELKRKAAQNSGE-AEYIEK 1674
Cdd:NF041483 964 AEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAR--EEADRTLDEARKDANKRRSEaAEQADT 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1675 VVYSVKQNADdvkkTLDGELDEKYKKVesliAQKTEESAD-----ARRKAELLQNEA----KTLLAQANSKL-QLLEDLE 1744
Cdd:NF041483 1042 LITEAAAEAD----QLTAKAQEEALRT----TTEAEAQADtmvgaARKEAERIVAEAtvegNSLVEKARTDAdELLVGAR 1113
|
570 580
....*....|....*....|....*...
gi 1666305206 1745 RkyedNQKYLEDKAQEL-VRLEGEVRSL 1771
Cdd:NF041483 1114 R----DATAIRERAEELrDRITGEIEEL 1137
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1020 |
1.89e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.27 E-value: 1.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1666305206 976 CQCHHNIDTTDPeaCDKETGRCLkCLYHTEGDHCQLCQYGYYGDA 1020
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-451 |
3.85e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 3.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 398 CTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLSAED 451
Cdd:smart00180 1 CDCDPGGSASGT-CDPDT--------GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
975-1026 |
5.87e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 5.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 975 PCQCHHNIDTtdPEACDKETGRCLkCLYHTEGDHCQLCQYGYYGDALR-QDCR 1026
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1453-1733 |
6.30e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.83 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKmvsEAKVR----ADEAKQNAQDVLLKTNATKEKV----DKSNEDLRNLIKQIRNFLTEDSadlDSIEAV 1524
Cdd:NF041483 182 AARAEAERLAE---EARQRlgseAESARAEAEAILRRARKDAERLlnaaSTQAQEATDHAEQLRSSTAAES---DQARRQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1525 ANEVLKmempSTPQQLQNLTEDIRE-RVETLSQVEVILQQSAADIARAELLLEEAKRASKSATdvkvtADMVKEALEEAE 1603
Cdd:NF041483 256 AAELSR----AAEQRMQEAEEALREaRAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEI-----ARLVGEATKEAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1604 KAQVAAEKAIkqADEDIQGTQNLLTSIE-SETAASEETltnASQrISKLERNVEELKRKAAQN--------SGEAEYI-- 1672
Cdd:NF041483 327 ALKAEAEQAL--ADARAEAEKLVAEAAEkARTVAAEDT---AAQ-LAKAARTAEEVLTKASEDakattraaAEEAERIrr 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1673 --EKVVYSVKQNADDVKKTLDGELDEKYKKVEsliAQKTEESADARRkaelLQNEAKTLLAQA 1733
Cdd:NF041483 401 eaEAEADRLRGEAADQAEQLKGAAKDDTKEYR---AKTVELQEEARR----LRGEAEQLRAEA 456
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-973 |
6.32e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 47.73 E-value: 6.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 917 CPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNPSDFGGSC 973
Cdd:pfam00053 1 CDCNPHGSLSDT----C--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
510-548 |
1.56e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 1.56e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1666305206 510 CDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-387 |
2.34e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 2.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 335 CNCNEHSS---SCHFDmavflatgnvsGGVCDnCQHNTMGRNCEQCKPFYFQHPER 387
Cdd:cd00055 2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
335-385 |
2.98e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 2.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 335 CNCNEHSS---SCHFdmavflatgnvSGGVCDnCQHNTMGRNCEQCKPFYFQHP 385
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1447-1749 |
4.61e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1447 FDRDVLSALAEVEQLSKMVSEAKVRA-DEAKQNAQDVLLKTNATKE--------KVDKSN-EDLRNLIKQIRNFLTEDSA 1516
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEEAEKKAkDQKEEDRRNYPTNTYKTLEleiaesdvEVKKAElELVKEEAKEPRDEEKIKQA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1517 DlDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAEL---LLEEAKRASKSATDVKVTAD 1593
Cdd:NF033838 210 K-AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgVLGEPATPDKKENDAKSSDS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1594 MVKE------------ALEEAEKAQVAAEKAIK-QADEDIQG-TQNLLTSIESETAASEETLTNASQRISKLE----RNV 1655
Cdd:NF033838 289 SVGEetlpspslkpekKVAEAEKKVEEAKKKAKdQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEEakepRNE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 EELKRKAAQ---NSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAEllqNEAKTLLAQ 1732
Cdd:NF033838 369 EKIKQAKAKvesKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPE---KPAEQPKAE 445
|
330
....*....|....*..
gi 1666305206 1733 ANSKLQLLEDLERKYED 1749
Cdd:NF033838 446 KPADQQAEEDYARRSEE 462
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
271-323 |
1.13e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.27 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 271 CFCYGHAS---ECAPVDGvneevegmvhgHCMCRHNTKGLNCELCMDFYHDLPWRP 323
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTG-----------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1456-1658 |
1.30e-05 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 48.00 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSN---EDLRNLIKQIRNFLT--EDSAD------LD-SIEA 1523
Cdd:cd11386 12 ASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVsavEELEESSAEIGEIVEviDDIAEqtnllaLNaAIEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 ------------VANEVLKMempstPQQLQNLTEDIRERVETLsqvevilqqsAADIARAellLEEAKRASKSATDVKVT 1591
Cdd:cd11386 92 arageagrgfavVADEVRKL-----AEESAEAAKEIEELIEEI----------QEQTEEA---VEAMEETSEEVEEGVEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1592 ADMVKEALEEaekaqvaaekaIKQADEDIQgtqnllTSIESETAASEEtLTNASQRISkleRNVEEL 1658
Cdd:cd11386 154 VEETGRAFEE-----------IVASVEEVA------DGIQEISAATQE-QSASTQEIA---AAVEEI 199
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
867-906 |
2.47e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1666305206 867 CQCN--GHALD-CDTVTGECLsCQDYTTGHNCERCLAGYYGDP 906
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-974 |
3.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 916 PCPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNPSDfGGSCQ 974
Cdd:cd00055 1 PCDCNGHGSLSGQ----C--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-388 |
5.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 5.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 335 CNCNE---HSSSCHFDmavflatgnvsGGVCDnCQHNTMGRNCEQCKPFYFQHPERD 388
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1019 |
9.59e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 976 CQCHHniDTTDPEACDKETGRCLkCLYHTEGDHCQLCQYGYYGD 1019
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| alph_xenorhab_B |
NF033927 |
alpha-xenorhabdolysin family binary toxin subunit B; |
1490-1732 |
1.05e-04 |
|
alpha-xenorhabdolysin family binary toxin subunit B;
Pssm-ID: 411488 [Multi-domain] Cd Length: 223 Bit Score: 45.70 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KEKVDKSNEDLRNLIKQIRN-FLTEDSADLdsieavanevlkmempstPQQLQNLTEDIRERVETLSQVEVILQQSAADI 1568
Cdd:NF033927 6 IAALRKSAAKIANKLDDLSQiNLREATLDL------------------LAQLQEQIAELEAQIAALESKLNELAEDRKVI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1569 ARAELLLEEAKrasksatdvkvTADMVKEAL---EEAEKAQVA-AEKAI-KQAdedIQGTQNLLTSIESetAASEETLTN 1643
Cdd:NF033927 68 IEAIDLIEKYN-----------IADLFKDLLptaEEIDSLGLPpPEKDLvKAA---IERLKKLLGKISE--GLTYIDLVE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1644 A----SQRISKLERNVEELKRKAAQNSGEAEYIeKVVYSVkqnaDDVKKTLDGEldekYKKVE----SLIAQKTEESADA 1715
Cdd:NF033927 132 ArdklRDRINALLAESRTLDKDIKALAGKLEEL-TAIAAI----DEERATWVAE----ARKVEqaweSFLDQLTELTSDS 202
|
250
....*....|....*..
gi 1666305206 1716 RRkaellQNEAKTLLAQ 1732
Cdd:NF033927 203 AN-----LAQLITQLNG 214
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1217-1604 |
2.26e-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: 46.00 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1217 RETVDSVEKKVNEI-KDILAQS----PAAEP----LKNIGILFEEAEKLT--------KDVTEKMAQvevkltdtasqsn 1279
Cdd:pfam06160 120 REEVEELKDKYRELrKTLLANRfsygPAIDElekqLAEIEEEFSQFEELTesgdyleaREVLEKLEE------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1280 stagELGALQAEAES----LDKTVKELAEQLEFIKN--------------SDIQGALDSITKYFQMSLEAEKRvnastTD 1341
Cdd:pfam06160 187 ----ETDALEELMEDipplYEELKTELPDQLEELKEgyremeeegyalehLNVDKEIQQLEEQLEENLALLEN-----LE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1342 PNSTVEQSALTRDRVEDL--MLERES----PFKEQQEEQARLLDELAGKLQSL--DLSAVAQmtcgtppgadcsesecgg 1413
Cdd:pfam06160 258 LDEAEEALEEIEERIDQLydLLEKEVdakkYVEKNLPEIEDYLEHAEEQNKELkeELERVQQ------------------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1414 pNCRTDEGEKKCGGPGCGGLVTV--AHSAWQKAMDFDRDVLSALAE--------VEQLSKMVSE-----AKVRADE--AK 1476
Cdd:pfam06160 320 -SYTLNENELERVRGLEKQLEELekRYDEIVERLEEKEVAYSELQEeleeileqLEEIEEEQEEfkeslQSLRKDEleAR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1477 QNAQDVLLKTNATKEKVDKSNedLRNLIKQIRNFLTEDSadlDSIEAVANEV--LKMEMPstpqQLQNLTEDIRERVETL 1554
Cdd:pfam06160 399 EKLDEFKLELREIKRLVEKSN--LPGLPESYLDYFFDVS---DEIEDLADELneVPLNMD----EVNRLLDEAQDDVDTL 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1666305206 1555 -SQVEVILQQSAAdiarAELLLEEAKR-ASKSATdvkvtadmVKEALEEAEK 1604
Cdd:pfam06160 470 yEKTEELIDNATL----AEQLIQYANRyRSSNPE--------VAEALTEAEL 509
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1688-1779 |
3.16e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 43.29 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1688 KTLDGELDEKYKKVESLIAQKteeSADARRKAELLQNEAKTLLAQANSKLQllEDLERKYEDNQKYLEDKAQELVRLEGE 1767
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKL---EKELQALQEKLQKEAATLSEEERQKKE--RELQKKQQELQRKQQEAQQDLQKRQQE 116
|
90
....*....|..
gi 1666305206 1768 vrsLLKDISEKV 1779
Cdd:COG2825 117 ---LLQPILEKI 125
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1241-1307 |
4.60e-04 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 40.42 E-value: 4.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1241 EPLKNIGilfEEAEKLTKDVTEKMAQVEV---KLTDTASQSNSTAGELGALQAEAESLDktvKELAEQLE 1307
Cdd:cd22301 2 ERLKNIK---KEAENLAKEIEDKMKRIEDlekRIQDLNKRKEDKANQLARLEKQVISLR---KEIVERVE 65
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1669-1775 |
5.44e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1669 AEYIEKVVYSVKQNADdvkktLDGELDEKYKKVESLIAQKTE----ESADARRKAELLQNEAKTLLAQANSKLQLLEDLE 1744
Cdd:pfam00038 14 ASYIDKVRFLEQQNKL-----LETKISELRQKKGAEPSRLYSlyekEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1666305206 1745 RKYEDNQ--------------KYLEDKAQELVRLEGEVRSLLKDI 1775
Cdd:pfam00038 89 QKYEDELnlrtsaendlvglrKDLDEATLARVDLEAKIESLKEEL 133
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1679-1778 |
1.31e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1679 VKQNADDVKKTLDgeldekykKVESLIAQKTEESADARRKAELL----QNEAKTL----LAQANSKLQlledleRKYEDN 1750
Cdd:PRK07353 41 IRTNRAEAKERLA--------EAEKLEAQYEQQLASARKQAQAViaeaEAEADKLaaeaLAEAQAEAQ------ASKEKA 106
|
90 100
....*....|....*....|....*....
gi 1666305206 1751 QKYLEDKAQE-LVRLEGEVRSLLKDISEK 1778
Cdd:PRK07353 107 RREIEQQKQAaLAQLEQQVDALSRQILEK 135
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-326 |
1.72e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 271 CFCYGHASECAPVDgvneevegMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEG 326
Cdd:pfam00053 1 CDCNPHGSLSDTCD--------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-966 |
2.19e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 917 CPCpdgpDSGRQFARSCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNP 966
Cdd:smart00180 1 CDC----DPGGSASGTC--DPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1693-1780 |
2.55e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ELDEKYKKVESLIAQKteeSADARRKAELLQNEAKTLLAQANSKLQllEDLERKYEDNQKYLEDKAQELVRLEGE----V 1768
Cdd:smart00935 22 QLEKEFKKRQAELEKL---EKELQKLKEKLQKDAATLSEAAREKKE--KELQKKVQEFQRKQQKLQQDLQKRQQEelqkI 96
|
90
....*....|..
gi 1666305206 1769 RSLLKDISEKVA 1780
Cdd:smart00935 97 LDKINKAIKEVA 108
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
2.64e-110 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 349.96 E-value: 2.64e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 35 CYPATGDLLIGRaqKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHetlnpdSHLIENVVTTFAPNRLKiWWQS 114
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 115 ENGV---ENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFpGISTGPMK--KVDDII 189
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 190 CDSRYSDIEPSTEGEVIFRAL--DPAFKIEDpYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIReKYYYAVYDMVV 267
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 1666305206 268 RG 269
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
8.77e-85 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 277.32 E-value: 8.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 29 GCAEGSCYPATGDLLIGRaqKLSVTSTCGLHKPEPYCI-VSHLQEDKKCFICDSRDPYHetlnpdSHLIENVVTTFAPNR 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 108 LKiWWQSEN---GVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSsDFGKAWGVYRYFAYDCESSFPGISTGPMKK 184
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 185 V--DDIICDSRYSDIEPSTEGEVIFRALDPAFKIED-PYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYA 261
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 1666305206 262 VYDMVVRG 269
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1714-1786 |
2.22e-38 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 137.99 E-value: 2.22e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1714 DARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL 1786
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTCL 73
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1716-1785 |
1.44e-24 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 98.51 E-value: 1.44e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1716 RRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTC 1785
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1456-1776 |
6.49e-20 |
|
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: 97.43 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSeaKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNL---IKQIRNFLTEDSADLDSIE----AVANEV 1528
Cdd:TIGR02168 220 AELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEIEELQkelyALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 LKMEmpstpQQLQNLTEDIRERVETLSQVEVILQQSAAdiaRAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVA 1608
Cdd:TIGR02168 298 SRLE-----QQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1609 AEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEyiEKVVYSVKQNADDVKK 1688
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1689 tldgELDEKYKKVESLIAQKtEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEV 1768
Cdd:TIGR02168 448 ----ELEELQEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
|
....*...
gi 1666305206 1769 RSLLKDIS 1776
Cdd:TIGR02168 523 GVLSELIS 530
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1715-1785 |
7.33e-18 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 79.41 E-value: 7.33e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 1715 ARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTC 1785
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTC 71
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1446-1781 |
8.16e-18 |
|
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: 90.51 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1446 DFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAqDVLLKTNATKEKVDKSNEDLRNLIKQIRnfLTEDSADLDSIEAVA 1525
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYEGYEL--LKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1526 NEVLKMEmpstpQQLQNLTEDIRERVETLSQVEVILQQSAADIARaeLLLEEAKRASKSATDVKVTADMVKEALEEAEKA 1605
Cdd:TIGR02169 244 RQLASLE-----EELEKLTEEISELEKRLEEIEQLLEELNKKIKD--LGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1606 QVAAEKAIKQADEDIQGTQ----NLLTSIESET---AASEETLTNASQRISKLERNVEELKRKAA----QNSGEAEYIEK 1674
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLaeieELEREIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAetrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1675 V---VYSVKQNAD---DVKKTLDGELDEKYKKVESLIAQKTE---ESADARRKAELLQNEAKTLLAQANSKLQLLEDLER 1745
Cdd:TIGR02169 397 LkreINELKRELDrlqEELQRLSEELADLNAAIAGIEAKINEleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
330 340 350
....*....|....*....|....*....|....*.
gi 1666305206 1746 KYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAV 1781
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1457-1778 |
2.22e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1457 EVEQLSKMVSEAKvRADEAKQNAQDVLLKTNATKEKVDKSNEdlrnlikqirnfltEDSADLDSIEAVANEVLKMEMPST 1536
Cdd:PTZ00121 1303 KADEAKKKAEEAK-KADEAKKKAEEAKKKADAAKKKAEEAKK--------------AAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1537 PQQLQnlTEDIRERVETLsqvevilQQSAADIARAEllleEAKrasKSATDVKVTADMVKEALEEAEKAQVAAEKA--IK 1614
Cdd:PTZ00121 1368 AAEKK--KEEAKKKADAA-------KKKAEEKKKAD----EAK---KKAEEDKKKADELKKAAAAKKKADEAKKKAeeKK 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1615 QADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKaAQNSGEAEYIEKVVYSVKQNADDVKKTLDGEL 1694
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1695 D-EKYKKVESliAQKTEES--ADARRKAELLQNEAKTLLAQANSKLQLLEDLE--RKYEDNQKYLEDKAQELVRLEgevr 1769
Cdd:PTZ00121 1511 KaDEAKKAEE--AKKADEAkkAEEAKKADEAKKAEEKKKADELKKAEELKKAEekKKAEEAKKAEEDKNMALRKAE---- 1584
|
....*....
gi 1666305206 1770 sLLKDISEK 1778
Cdd:PTZ00121 1585 -EAKKAEEA 1592
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
773-818 |
1.28e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 72.34 E-value: 1.28e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGC 818
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
821-869 |
1.63e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.00 E-value: 1.63e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 821 CDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPSCQPCQC 869
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1778 |
3.57e-15 |
|
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: 79.42 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1559 VILQQSAADIARAELLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAEL----------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1639 ETLTNASQRISKLERNVEELKRK------AAQNSGEAEYIE------------KVVYSVKQNADDVKKTLDgELDEKYKK 1700
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaellrALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1701 VESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
773-821 |
7.90e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 70.07 E-value: 7.90e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPC 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1224-1781 |
9.34e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1224 EKKVNEIKDILAQSPAAEPLKNIGILFEE---AEKLTKDVTEKMAQV-----EVKLTDTASQSNSTAGELGALQAEAESL 1295
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEarkADELKKAEEKKKADEakkaeEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1296 DKTVKELAEQLEFIKNSDiQGALDSITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESpfKEQQEEQA 1375
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA--KKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1376 RLLDELAGKLQSLDLSAVAQMTCGTPPGADCSESecggpncRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDR-DVLSA 1454
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-------KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKaDEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1455 LAE----VEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNlikqirnflTEDSADLDSIEAvANEVLK 1530
Cdd:PTZ00121 1478 KAEeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---------AEEAKKADEAKK-AEEKKK 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1531 MEMPSTPQQLQNLTEdiRERVETLSQVEvilQQSAADIARAELLLE-EAKRASKSATDVKVTADMVKEALEEAEKAQVAA 1609
Cdd:PTZ00121 1548 ADELKKAEELKKAEE--KKKAEEAKKAE---EDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1610 EKaIKQADEDIQGTQNLLTSIESET-------AASEETLTNASQRISKLE---RNVEELKR-------KAAQNSGEAEYI 1672
Cdd:PTZ00121 1623 EE-LKKAEEEKKKVEQLKKKEAEEKkkaeelkKAEEENKIKAAEEAKKAEedkKKAEEAKKaeedekkAAEALKKEAEEA 1701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1673 EKVVYSVKQNADDVKKT--LDGELDEKYKKVESLIAQKTEEsadaRRKAEllqnEAKTLLAQANSKLQLLEDLERKYEDN 1750
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEED----KKKAE----EAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
570 580 590
....*....|....*....|....*....|....*.
gi 1666305206 1751 QKYLEDKAQELVRLEGEVRSL-----LKDISEKVAV 1781
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMevdkkIKDIFDNFAN 1809
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-819 |
1.12e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.12e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 772 ACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGF--GPNGCK 819
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1189-1747 |
1.26e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1189 IIGELTNRTHKFLEKAKALKISgvigpYRETVDSVEKKVNEIKDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVE 1268
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEK-----IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1269 VKLTDTASQSNSTAGELgalqAEAESLDKTVKELAEQLEFIKNSdiQGALDSITKYFQMSLEAEKRVNASTTdpnstvEQ 1348
Cdd:PRK03918 314 KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKK------RL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1349 SALTRDRVEDLMLERESPFKEQQEEqarlLDELAGKLQSLD------LSAVAQMTcgtppGAdcsESECggPNCR---TD 1419
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEE----ISKITARIGELKkeikelKKAIEELK-----KA---KGKC--PVCGrelTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1420 EGEKKCGGPGCGGLVTVAhSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQ--NAQDVLLKTNATK-----EK 1492
Cdd:PRK03918 448 EHRKELLEEYTAELKRIE-KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNLEElekkaEE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1493 VDKSNEDLRNLIKQIRNFLTEdsadLDSIEAVANE--VLKMEMPSTPQQLQNLTEDIRER-VETLSQVEVILQQsaadia 1569
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKlaELEKKLDELEEELAELLKELEELgFESVEELEERLKE------ 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 raellLEEAKRASKSATDVKvtadmvKEaLEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAA-----SEETLTNA 1644
Cdd:PRK03918 597 -----LEPFYNEYLELKDAE------KE-LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEEL 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1645 SQRISKLERnveELKRKAAqnsgEAEYIEKVVYSVKQNADDVKKTLDgELDEKYKKVEsLIAQKTEESADARRKAELLQN 1724
Cdd:PRK03918 665 REEYLELSR---ELAGLRA----ELEELEKRREEIKKTLEKLKEELE-EREKAKKELE-KLEKALERVEELREKVKKYKA 735
|
570 580
....*....|....*....|....*.
gi 1666305206 1725 EAKTLLAQANSKL--QLLEDL-ERKY 1747
Cdd:PRK03918 736 LLKERALSKVGEIasEIFEELtEGKY 761
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1453-1777 |
5.26e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKMVSEAKVRADEAKQNAQDVLL-----------------KTNATKEKVDKSNEDLRNLIKQIRNFLTE-- 1513
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEeheerreeletleaeieDLRETIAETEREREELAEEVRDLRERLEEle 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1514 -------DSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERV-ETLSQVEViLQQSAADIA-RAELLLEEAKRASKS 1584
Cdd:PRK02224 293 eerddllAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAqAHNEEAES-LREDADDLEeRAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1585 ATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESE-------TAASEETLTNASQRISKLER---- 1653
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrerEAELEATLRTARERVEEAEAllea 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1654 -----------------NVEELKRKAAQNSGEAEYIEKVVYSVKQN---ADDVKKTLDG--ELDEKYKKVESLIAQKTEE 1711
Cdd:PRK02224 452 gkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERlerAEDLVEAEDRieRLEERREDLEELIAERRET 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1666305206 1712 SADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQ---KYLEDKAQELV-RLEG--EVRSLLKDISE 1777
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevAELNSKLAELKeRIESleRIRTLLAAIAD 603
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1541-1778 |
7.49e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1541 QNLT--EDIRE----RVETLS-QVEVILQ----QSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAA 1609
Cdd:COG1196 186 ENLErlEDILGelerQLEPLErQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1610 EKAIKQADEDI----------QGTQNLLTS----IESETAASEETLTNASQRISKLERNVEELKRKAAQNS-------GE 1668
Cdd:COG1196 266 EAELEELRLELeeleleleeaQAEEYELLAelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEeeleeleEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1669 AEYIEKVVYSVKQNADDVKKTLDgELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYE 1748
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270
....*....|....*....|....*....|
gi 1666305206 1749 DNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1538-1782 |
1.72e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKrasksatdvkvtadmvkEALEEAEKAQVAAEKAIKQAD 1617
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-----------------LELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1618 EDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEK 1697
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1698 YKKVESLIAQKTEESADARRKAEL------LQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSL 1771
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELeeaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250
....*....|.
gi 1666305206 1772 LKDISEKVAVY 1782
Cdd:COG1196 462 LELLAELLEEA 472
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1467-1769 |
3.86e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1467 EAKVRADEAKQNAQDvllktnATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEA-VANEVLKMEMPSTPQQLQNlTE 1545
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAKK-AE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1546 DIRERVEtlsqveviLQQSAADIARAELLLEEAKRASKSATDVKvtadmvKEALEEAEKAQVAAEKAIKQADEdiqgtqn 1625
Cdd:PTZ00121 1300 EKKKADE--------AKKKAEEAKKADEAKKKAEEAKKKADAAK------KKAEEAKKAAEAAKAEAEAAADE------- 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1626 lltsieseTAASEETLTNASQRISKLERNVEELKRKAAQNSgEAEYIEKVVYSVKQNADDVKKTLDG--ELDEKYKKVES 1703
Cdd:PTZ00121 1359 --------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAkkKADEAKKKAEE 1429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1704 L-IAQKTEESADARRKAELLQNEAKTLLAQANSKLQL-----LEDLERKYEDNQKY--LEDKAQELVRLEGEVR 1769
Cdd:PTZ00121 1430 KkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakkADEAKKKAEEAKKAdeAKKKAEEAKKKADEAK 1503
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1718-1785 |
7.10e-13 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 65.07 E-value: 7.10e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1718 KAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTC 1785
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1433-1779 |
1.04e-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: 73.55 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1433 LVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMV---SEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRN 1509
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1510 FLTEDSADLDSIEAvanevlkmempstpqQLQNLTEDIRERVETLSQVEvilQQSAADIARAELLLEEAKRASKSATDVK 1589
Cdd:TIGR02168 797 ELKALREALDELRA---------------ELTLLNEEAANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1590 vtadmvkEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQnsgea 1669
Cdd:TIGR02168 859 -------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----- 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1670 eyIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTL-------LAQANSKLQLLED 1742
Cdd:TIGR02168 927 --LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDF 1004
|
330 340 350
....*....|....*....|....*....|....*..
gi 1666305206 1743 LERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKV 1779
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQV 1041
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1716-1785 |
1.21e-12 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 64.56 E-value: 1.21e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1716 RRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTC 1785
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1251-1773 |
2.32e-12 |
|
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: 72.52 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEA-------EKLTKDvtEKMAQVEVKLTDTASQSNStagelgaLQAEAESLDKTVKE----LAEQLEFIKN-------- 1311
Cdd:pfam01576 115 EEAarqklqlEKVTTE--AKIKKLEEDILLLEDQNSK-------LSKERKLLEERISEftsnLAEEEEKAKSlsklknkh 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1312 ----SDIQGALDSITKYFQmSLEAEKR-VNASTTDPNstvEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQ 1386
Cdd:pfam01576 186 eamiSDLEERLKKEEKGRQ-ELEKAKRkLEGESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1387 SLdlSAVAQMTCGTPPGADCSESECGGPN----CRTDEGEKKCGGPGCGgLVTVAHSAWQKAMDFDRDvlsalAEVEQLS 1462
Cdd:pfam01576 262 AL--KKIRELEAQISELQEDLESERAARNkaekQRRDLGEELEALKTEL-EDTLDTTAAQQELRSKRE-----QEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1463 KMVSEaKVRADEAKqnAQDVLLKTNATkekVDKSNEDLRNLiKQIRNFLTEDSADLDSieavANEVLKMEMpSTPQQLQN 1542
Cdd:pfam01576 334 KALEE-ETRSHEAQ--LQEMRQKHTQA---LEELTEQLEQA-KRNKANLEKAKQALES----ENAELQAEL-RTLQQAKQ 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1543 LTEDIRERVEtlSQV-EVILQQSAADIARAELlleeAKRASKSATDVkvtaDMVKEALEEAEKAQVAAEKAIKQADEDIQ 1621
Cdd:pfam01576 402 DSEHKRKKLE--GQLqELQARLSESERQRAEL----AEKLSKLQSEL----ESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1622 GTQNLLtsiesetaaSEETLT--NASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELdekyK 1699
Cdd:pfam01576 472 DTQELL---------QEETRQklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA----G 538
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1700 KVESLiaqktEEsadARRKaelLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLK 1773
Cdd:pfam01576 539 TLEAL-----EE---GKKR---LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1457-1778 |
3.48e-12 |
|
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: 71.59 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1457 EVEQLSKMVSEAKVRADEAKQNAQDvlLKtnatKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEvLKMEMPST 1536
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISD--LN----NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ-LNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1537 PQQLQNLTEDIRERVETL----SQVEVILQQSAAdiaraelLLEEAKRASKSATDVKVTADMVKEalEEAEKaqvaaEKA 1612
Cdd:TIGR04523 348 KKELTNSESENSEKQRELeekqNEIEKLKKENQS-------YKQEIKNLESQINDLESKIQNQEK--LNQQK-----DEQ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1613 IKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKtldg 1692
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ELDEKYKKVESLIAQKT---EESAD-ARRKAELLQNEAK--TLLAQANSKLQLLED--LERKYEDNQKYLED----KAQE 1760
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKeleEKVKDlTKKISSLKEKIEKleSEKKEKESKISDLEDelNKDDFELKKENLEKeideKNKE 569
|
330
....*....|....*...
gi 1666305206 1761 LVRLEGEVRSLLKDISEK 1778
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEK 587
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
3.63e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 3.63e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRAC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1498-1777 |
3.71e-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: 72.01 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1498 EDLRNLI-------------KQIRNFLTEDSADLDSIEAVANEVLKmempstpqQLQNL------TEDIRERVETLSQVE 1558
Cdd:TIGR02168 155 EERRAIFeeaagiskykerrKETERKLERTRENLDRLEDILNELER--------QLKSLerqaekAERYKELKAELRELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1559 VILQqsaadIARAELLLEEAKRasksatdvkvtadmVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:TIGR02168 227 LALL-----VLRLEELREELEE--------------LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1639 ETLTNASQRISKLERNVEELKRKaaqnsgeaeyiekvvysvKQNADDVKKTLDGELDEKYKKVESLIaqktEESADARRK 1718
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRER------------------LANLERQLEELEAQLEELESKLDELA----EELAELEEK 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1719 AELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1455-1780 |
6.25e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1455 LAEVEQLSKMVSEAKVRADEAKQnAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLtedsADLDSIEAVANevLKMEMP 1534
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLL----QLLPLYQELEA--LEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1535 STPQQLQNLtediRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSAT-----DVKVTADMVKEALEEAEKAQVAA 1609
Cdd:COG4717 143 ELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelqDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1610 EKAIKQADEDIQGTQNlltsiESETAASEETLTNASQRI----------------------------------------- 1648
Cdd:COG4717 219 QEELEELEEELEQLEN-----ELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallflll 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1649 ----SKLERNVEELKRKAAQNSGEAEYIEKVVySVKQNADDVKKTLDGELDEKYKKVESLIAQKteESADARRKAELLQN 1724
Cdd:COG4717 294 arekASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 1725 EAKTLLAQANSKlqLLEDLERKYEDNQKYLEDKaQELVRLEGEVRSLLKDISEKVA 1780
Cdd:COG4717 371 EIAALLAEAGVE--DEEELRAALEQAEEYQELK-EELEELEEQLEELLGELEELLE 423
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
820-863 |
7.75e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 7.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 820 PCDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPS 863
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1132-1171 |
8.67e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 8.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1666305206 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSG 1171
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1483-1771 |
1.07e-11 |
|
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: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1483 LLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLD----SIEAVANEV--LKMEMPSTPQQLQNLTEDIRERVETLSQ 1556
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdasrKIGEIEKEIeqLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1557 VEVILQQSAADIARAELLLEEAKRASKS--ATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESET 1634
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1635 AASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYsvkqnaddvkkTLDGELDEKYKKVESLIAQKtEESAD 1714
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----------DLESRLGDLKKERDELEAQL-RELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1715 ARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKY----------LEDKAQELVRLEGEVRSL 1771
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRAL 970
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1442-1752 |
1.94e-11 |
|
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: 69.28 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1442 QKAMDFDRDVLSALAEVEqlskmvseakvradEAKQNAQDVLLKTNatkEKVDKSNEDLRNLIKQIRNFLTEDSADLDSI 1521
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQE--------------KKLEEIQNQISQNN---KIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1522 EAVANEV--LKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAE----LLLEEAKRASKSATDVKVT---- 1591
Cdd:TIGR04523 366 EEKQNEIekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNNSEikdl 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 --ADMVKE-------ALEEAEKAQVAA-EKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRK 1661
Cdd:TIGR04523 446 tnQDSVKEliiknldNTRESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1662 AAQNSGEAEYIEKVVYSVKQ--NADDVKKT---LDGELDEKYKKVESLIAQKTEESADARRKAELLQN---EAKTLLAQA 1733
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDelNKDDFELKkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQkekEKKDLIKEI 605
|
330
....*....|....*....
gi 1666305206 1734 NSKLQLLEDLERKYEDNQK 1752
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKK 624
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1285-1773 |
2.10e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1285 LGALQAEAESLDKTVKELAEQLEFIKNSdiQGALDSITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERE 1364
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARET--RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1365 SPFKEQQEEQARLLDELAgkLQSLDLSAVAQ----------------MTCGTPPGADCSESECGGPNCRTDEGEKKCGGP 1428
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG--LDDADAEAVEArreeledrdeelrdrlEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1429 GCGGLVTVAHSAWQKAMDFdRDVLSAL-AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQI 1507
Cdd:PRK02224 364 EAAELESELEEAREAVEDR-REEIEELeEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1508 R------------------------NFLTED-------SADLDSIEAVANEV-LKMEMPSTPQQLQNLTEDIRERVETLs 1555
Cdd:PRK02224 443 EeaealleagkcpecgqpvegsphvETIEEDrerveelEAELEDLEEEVEEVeERLERAEDLVEAEDRIERLEERREDL- 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1556 qVEVILQQSA---ADIARAELLLEEAKRASKSATDVKVTADmvkEALEEAEKAQVAAeKAIKQADEDIQGTQNLLTSIES 1632
Cdd:PRK02224 522 -EELIAERREtieEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEV-AELNSKLAELKERIESLERIRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1633 etaaSEETLTNASQRISKLErnvEELKRKAAQNSGEAEYI-EKvvysvkqnaDDVKKTLDGELDE--------KYKKVES 1703
Cdd:PRK02224 597 ----LLAAIADAEDEIERLR---EKREALAELNDERRERLaEK---------RERKRELEAEFDEarieeareDKERAEE 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 1704 LIAQKTEESADARRKAELLQNEaktlLAQANSKLQLLEDL--ERK-YEDNQKYLE---DKAQELVRLEGEVRSLLK 1773
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAE----IGAVENELEELEELreRREaLENRVEALEalyDEAEELESMYGDLRAELR 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1456-1778 |
2.72e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEakqnaqdvLLKTNATKEKVDKSNEDLRNLIKQIRNF----------LTEDSADLDSIEAVA 1525
Cdd:PRK03918 221 EELEKLEKEVKELEELKEE--------IEELEKELESLEGSKRKLEEKIRELEERieelkkeieeLEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1526 NEVLKM----------------EMPSTPQQLQNLTEDIRE------RVETLSQVEVILQQSAADIARAELLLEEAKRASK 1583
Cdd:PRK03918 293 EEYIKLsefyeeyldelreiekRLSRLEEEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1584 SATDVK-----VTADMVKEALEEAEKAQVAAEKAIKQADEDIQGtqnlLTSIESETAASEETLTNASQRISKLERNVEEL 1658
Cdd:PRK03918 373 ELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1659 KRKaaqnsgeaEYIEKVVYSVKQNADDVKKTLDGE--LDEKYKKVESLIAQKTEESADaRRKAELLQNEAKTLlaqanSK 1736
Cdd:PRK03918 449 HRK--------ELLEEYTAELKRIEKELKEIEEKErkLRKELRELEKVLKKESELIKL-KELAEQLKELEEKL-----KK 514
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1666305206 1737 LQlLEDLERKYEDNQKYLEdkaqELVRLEGEVRSLLKDISEK 1778
Cdd:PRK03918 515 YN-LEELEKKAEEYEKLKE----KLIKLKGEIKSLKKELEKL 551
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1478-1783 |
2.72e-11 |
|
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: 68.45 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1478 NAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSAD----LDSIEAVANEVLKmempstpqQLQNLTEDIRERVET 1553
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGEnaesSKRLNENANNLIK--------QFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1554 LSQVEVILQQSAAdIARAELL--LEEAKRASKSatdvkvtadMVKEALEEAEKAQVAAEKAIKQADEDIQgtqNLLTSIE 1631
Cdd:COG5185 305 IDIKKATESLEEQ-LAAAEAEqeLEESKRETET---------GIQNLTAEIEQGQESLTENLEAIKEEIE---NIVGEVE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1632 SETaaSEETLTNASQRIsklERNVEEL--KRKAAQNSGeaeyiekvvysvKQNADDVKKTLdGELDEKYKKVESLIAQKT 1709
Cdd:COG5185 372 LSK--SSEELDSFKDTI---ESTKESLdeIPQNQRGYA------------QEILATLEDTL-KAADRQIEELQRQIEQAT 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 1710 EESADARRKAELLQNEA--KTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYS 1783
Cdd:COG5185 434 SSNEEVSKLLNELISELnkVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLE 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1476-1775 |
2.95e-11 |
|
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: 68.51 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1476 KQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRN----------------------------FLTE---DSADLDSIEAV 1524
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNdkeqknklevelnklekqkkenkknidkFLTEikkKEKELEKLNNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1525 ANEVLKmempstpqQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLL-------EEAKRASKSATDVKVTADMVKE 1597
Cdd:TIGR04523 161 YNDLKK--------QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiQKNKSLESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1598 ALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRK-AAQNSGEAEYIEKVV 1676
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEiSDLNNQKEQDWNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1677 YSVKQNADDVKKTLDGELDEKYKKVESL---IAQ-KTE----ESADARRKAELL--QNEAKTLLAQANSKLQLLE----- 1741
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLneqISQlKKEltnsESENSEKQRELEekQNEIEKLKKENQSYKQEIKnlesq 392
|
330 340 350
....*....|....*....|....*....|....*.
gi 1666305206 1742 --DLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDI 1775
Cdd:TIGR04523 393 inDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1459-1778 |
3.43e-11 |
|
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: 68.51 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKQNaqDVLLKTNAT----KEK-VDKSNEDLRNLIKQIR---NFLTEDSADLDSIEA----VAN 1526
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKEN--KKNIDKFLTeikkKEKeLEKLNNKYNDLKKQKEeleNELNLLEKEKLNIQKnidkIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1527 EVLKME-----MPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKrasKSATDVKVTADMVKEALEE 1601
Cdd:TIGR04523 195 KLLKLElllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ---TQLNQLKDEQNKIKKQLSE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 AEKAQVAAEKAIKQADEDI------------QGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQnsgea 1669
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ----- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1670 eyIEKvvysVKQNADDVKKTLDGELDEKYKKVESLI---AQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERK 1746
Cdd:TIGR04523 347 --LKK----ELTNSESENSEKQRELEEKQNEIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420
|
330 340 350
....*....|....*....|....*....|..
gi 1666305206 1747 YEDNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1446-1777 |
3.94e-11 |
|
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: 68.56 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1446 DFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNL---IKQIRNFLTEDSADLDSIE 1522
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1523 A-----------VANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSatdvkvt 1591
Cdd:TIGR02169 765 ArieeleedlhkLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE------- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 admvKEALEEAEKAQvaaEKAIKQADEDIQGTQNLLTSIESETAASEETLtnaSQRISKLERNVEELK---RKAAQNSGE 1668
Cdd:TIGR02169 838 ----LQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEELEAALRDL---ESRLGDLKKERDELEaqlRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1669 AEY-IEKVvysvKQNADDVKKTLdGELDEKYKKVESLIAQKTEESAdARRKAELLQNEAKTLLAqansKLQLLEDL---- 1743
Cdd:TIGR02169 908 LEAqIEKK----RKRLSELKAKL-EALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEE----EIRALEPVnmla 977
|
330 340 350
....*....|....*....|....*....|....
gi 1666305206 1744 ERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
821-864 |
4.29e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.29e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 821 CDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWG--FPSC 864
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1132-1176 |
4.92e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 4.92e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGV-FPDC 1176
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1131-1180 |
7.20e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 7.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1131 ACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCH 1180
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1126 |
8.84e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 8.84e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 1083 PCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPD 1126
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1217-1777 |
9.33e-11 |
|
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: 67.40 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1217 RETVDSVEKKVNEIKDILAqspaaEPLKNIGILFEEAEKLTK--DVTEKMAQVEVKLTdtasqsnstAGELGALQAEAES 1294
Cdd:TIGR02169 176 LEELEEVEENIERLDLIID-----EKRQQLERLRREREKAERyqALLKEKREYEGYEL---------LKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1295 LDKTVKELAEQLEFIKnSDIQGALDSITKYFQMSLEAEKRVNASTTDpnstvEQSALTRdRVEDLMLERESpFKEQQEEQ 1374
Cdd:TIGR02169 242 IERQLASLEEELEKLT-EEISELEKRLEEIEQLLEELNKKIKDLGEE-----EQLRVKE-KIGELEAEIAS-LERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1375 ARLLDELAGKLQSLdlsavaqmtcgtppgadcsESECGgpncRTDEgekkcggpgcgglvtvahsawqKAMDFDRDVLSA 1454
Cdd:TIGR02169 314 ERELEDAEERLAKL-------------------EAEID----KLLA----------------------EIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1455 LAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEV--LKME 1532
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELadLNAA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1533 MPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADI--ARAEL--LLEEAKRASKSATDVKVTADMV---KEALEEAEKA 1605
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskYEQELydLKEEYDRVEKELSKLQRELAEAeaqARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1606 QVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLtnASQRISKL--------ERNVEELKRKaaqNSGEAEYI----- 1672
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVA--AGNRLNNVvveddavaKEAIELLKRR---KAGRATFLplnkm 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1673 -----------------------------EKVVYSV------KQNADDVKK--------TLDGELDEK------------ 1697
Cdd:TIGR02169 584 rderrdlsilsedgvigfavdlvefdpkyEPAFKYVfgdtlvVEDIEAARRlmgkyrmvTLEGELFEKsgamtggsrapr 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1698 ---------------------------------YKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLE 1744
Cdd:TIGR02169 664 ggilfsrsepaelqrlrerleglkrelsslqseLRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670
....*....|....*....|....*....|...
gi 1666305206 1745 RKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1466-1778 |
1.13e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.58 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1466 SEAKVRADeakQNAQDVLLKTNATkekVDKSNEDLRNLIKQIRnfltedSADLdsIEAVANEV-LKMEMPSTPQQLQNLT 1544
Cdd:COG3206 55 ASATLLVE---PQSSDVLLSGLSS---LSASDSPLETQIEILK------SRPV--LERVVDKLnLDEDPLGEEASREAAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1545 EDIRERVETLSQ-----VEVILQ----QSAADIARA--ELLLEEAKRASKSATdvKVTADMVKEALEEAEKAQVAAEKAI 1613
Cdd:COG3206 121 ERLRKNLTVEPVkgsnvIEISYTspdpELAAAVANAlaEAYLEQNLELRREEA--RKALEFLEEQLPELRKELEEAEAAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1614 K--QADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEK--VVYSVKQNADDVKKT 1689
Cdd:COG3206 199 EefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1690 LDgELDEKYK----KVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLE 1765
Cdd:COG3206 279 LA-ELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE 357
|
330
....*....|....*.
gi 1666305206 1766 GEV---RSLLKDISEK 1778
Cdd:COG3206 358 REVevaRELYESLLQR 373
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1201-1760 |
1.45e-10 |
|
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: 66.74 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1201 LEKAKALKISgvigpYRETVDSVEKKVNEIkdilaqspaAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNS 1280
Cdd:pfam01576 365 LEQAKRNKAN-----LEKAKQALESENAEL---------QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1281 TAGELGALQAEAESLDKTVKELAEQLefIKNSDIQGALDSITKYFQMSLEAEKR--VNASTtdpnstveqsaltrdRVED 1358
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKN--IKLSKDVSSLESQLQDTQELLQEETRqkLNLST---------------RLRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1359 LMLERESpFKEQQEEQARLLDELAGKLQSLDlsavAQMtcgtppgadcsesecggpncrtdegekkcggpgcgglvtvah 1438
Cdd:pfam01576 494 LEDERNS-LQEQLEEEEEAKRNVERQLSTLQ----AQL------------------------------------------ 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1439 SAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTnatKEKVDKSNEDL-----------RNLIKQI 1507
Cdd:pfam01576 527 SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT---KNRLQQELDDLlvdldhqrqlvSNLEKKQ 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1508 RNF---LTEDSA-------DLDSIEAVANE----VLkmempSTPQQLQNLTEDIRE--RVETLSQVEV-ILQQSAADIAR 1570
Cdd:pfam01576 604 KKFdqmLAEEKAisaryaeERDRAEAEAREketrAL-----SLARALEEALEAKEEleRTNKQLRAEMeDLVSSKDDVGK 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1571 AELLLEEAKRASKS-ATDVKVTADMVKEALEEAEKAQVAAE---KAIK-QADEDIQG--TQN------LLTSI-ESETAA 1636
Cdd:pfam01576 679 NVHELERSKRALEQqVEEMKTQLEELEDELQATEDAKLRLEvnmQALKaQFERDLQArdEQGeekrrqLVKQVrELEAEL 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1637 SEE----TLTNASQRisKLERNVEELKRKA-AQNSGEAEYIE---KVVYSVK---QNADDVKKTLD------GELDEKYK 1699
Cdd:pfam01576 759 EDErkqrAQAVAAKK--KLELDLKELEAQIdAANKGREEAVKqlkKLQAQMKdlqRELEEARASRDeilaqsKESEKKLK 836
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1700 KVESLIAQKTEE---SADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQE 1760
Cdd:pfam01576 837 NLEAELLQLQEDlaaSERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEE 900
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1223-1783 |
1.57e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1223 VEKKVNEIKDILAQSpaaeplknigilfEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTvKEL 1302
Cdd:PRK03918 174 IKRRIERLEKFIKRT-------------ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1303 AEQLEfIKNSDIQGALDSITKYFQmslEAEKRVNasttdpnSTVEQSALTRDRVEDLmlERESPFKEQQEEQARLLDELA 1382
Cdd:PRK03918 240 IEELE-KELESLEGSKRKLEEKIR---ELEERIE-------ELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1383 GKLQSLD--LSAVaqmtcgtppgadcsESECGGPNCRTDEGEKKCGGPGCGGlvtvahsawQKAMDFDRDvLSALAEVEQ 1460
Cdd:PRK03918 307 DELREIEkrLSRL--------------EEEINGIEERIKELEEKEERLEELK---------KKLKELEKR-LEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1461 LSKMVSEAKVRADEAKQNaqdvllKTNATKEKVDKSNEDLRNLIKQIR---NFLTEDSADLDSIEA---VANEVLKMEMP 1534
Cdd:PRK03918 363 LYEEAKAKKEELERLKKR------LTGLTPEKLEKELEELEKAKEEIEeeiSKITARIGELKKEIKelkKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1535 STPQQLQNLTEDirERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDV----------KVTADMVKEALEEAEK 1604
Cdd:PRK03918 437 KCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeseliklKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1605 aqVAAEKaIKQADEDIQGTQNLLTSIESEtaaseetltnasqrISKLErnvEELKRKAAQNSGEAEYIEKvvysvkqnad 1684
Cdd:PRK03918 515 --YNLEE-LEKKAEEYEKLKEKLIKLKGE--------------IKSLK---KELEKLEELKKKLAELEKK---------- 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1685 dvKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLaqaNSKlQLLEDLERKYEDNQKYLEDKAQELVRL 1764
Cdd:PRK03918 565 --LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK---DAE-KELEREEKELKKLEEELDKAFEELAET 638
|
570
....*....|....*....
gi 1666305206 1765 EGEVRSLLKDISEKVAVYS 1783
Cdd:PRK03918 639 EKRLEELRKELEELEKKYS 657
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1534-1784 |
1.78e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.92 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1534 PSTPQQLQNLTEDIRERVETLSQVevilqQSAADIARAELlleEAKRASKSAtdvkvtadmVKEALEEAEKAQVAAEKAI 1613
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKL-----QEELEQLREEL---EQAREELEQ---------LEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1614 KQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVysvkQNADDVKKTLDGE 1693
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI----AEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1694 LDEKYKKVESLiaqkteESADARRKAELLQNEAKTLLAQANSKLQLLEDLErkyEDNQKYLEDKAQELVRLEGEVRSLLK 1773
Cdd:COG4372 159 LESLQEELAAL------EQELQALSEAEAEQALDELLKEANRNAEKEEELA---EAEKLIESLPRELAEELLEAKDSLEA 229
|
250
....*....|.
gi 1666305206 1774 DISEKVAVYST 1784
Cdd:COG4372 230 KLGLALSALLD 240
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1223-1764 |
2.05e-10 |
|
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: 66.22 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1223 VEKKVNEIKDILAQSPAAE-PLKNIGILFEEAEKLTKDVT--EKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKT- 1298
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEgSSDRILELDQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLn 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1299 ------------VKELAEQLEFIKNSDIQGA--LDSITKYFQMSLEAEKRVNASTTDPNstveqsaLTRDRVEDLMLERE 1364
Cdd:TIGR00606 529 hhtttrtqmemlTKDKMDKDEQIRKIKSRHSdeLTSLLGYFPNKKQLEDWLHSKSKEIN-------QTRDRLAKLNKELA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1365 SpfKEQQEEQARllDELAGKL-QSLDLSAVAQMTCGtppgadCSESECGGPNCRTDegekkcggpgcgglvtVAHSAWQK 1443
Cdd:TIGR00606 602 S--LEQNKNHIN--NELESKEeQLSSYEDKLFDVCG------SQDEESDLERLKEE----------------IEKSSKQR 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1444 AMdfdrdvLSALAEVeqLSKMVSEAKvradEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEA 1523
Cdd:TIGR00606 656 AM------LAGATAV--YSQFITQLT----DENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 VANEVLKMeMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLE----EAKRASKSATDVKVTaDMVKEAL 1599
Cdd:TIGR00606 724 RRDEMLGL-APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimpEEESAKVCLTDVTIM-ERFQMEL 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1600 EEAEK--AQVAAE-------KAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRK-------AA 1663
Cdd:TIGR00606 802 KDVERkiAQQAAKlqgsdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqigtnLQ 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1664 QNSGEAEYIEKVVYSVKQNADDVKKTLDGEL-DEKYKK-----VESLIAQKTEESADARRKAELLQNEAKtllaqanSKL 1737
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEkdqqeKEELISSKETSNKKAQDKVNDIKEKVK-------NIH 954
|
570 580
....*....|....*....|....*...
gi 1666305206 1738 QLLEDLERKYEDN-QKYLEDKAQELVRL 1764
Cdd:TIGR00606 955 GYMKDIENKIQDGkDDYLKQKETELNTV 982
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1129 |
3.83e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.83e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1666305206 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVEC 1129
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-508 |
4.06e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 4.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1666305206 457 SCACNPLGTIPGGnpCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCR 508
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1028-1082 |
4.25e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1028 CVCNYLGTVKEHCngsdchcDKATGQCSCLPNVIGQNCDRCAPNTWQLASGTGCG 1082
Cdd:pfam00053 1 CDCNPHGSLSDTC-------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1188-1675 |
4.33e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1188 AIIGELTNRTHKflEKAKALKISGVIGP-YRETVDSVEKKVNEIKDILAQ-SPAAEPLKNIGILFEEAEKLTKDVTEKMA 1265
Cdd:COG4717 42 FIRAMLLERLEK--EADELFKPQGRKPElNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1266 QVEVKLtdtasQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKN--SDIQGALDSITKYFQmSLEAEKRVNASTTDpn 1343
Cdd:COG4717 120 KLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELREleEELEELEAELAELQE-ELEELLEQLSLATE-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1344 STVEQSALTRDRVEDLMLERESPFKEQQEEQARL---LDELAGKLQSLDLSAVAQMTCGTPPGAdcSESECGGPNCRTDE 1420
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELeeeLEQLENELEAAALEERLKEARLLLLIA--AALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1421 GEKKCGGPGCGGLVTVAHSAWQKamdFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVD---KSN 1497
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLL---LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLellDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1498 EDLRNLIKQIRNflTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQsaadiaraellLEE 1577
Cdd:COG4717 347 EELQELLREAEE--LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-----------LEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1578 AKRASKSATDvKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLtsiesETAASEETLTNASQRISKLERNVEE 1657
Cdd:COG4717 414 LLGELEELLE-ALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQELEELKAELRE 487
|
490
....*....|....*...
gi 1666305206 1658 LKRKAAQNSGEAEYIEKV 1675
Cdd:COG4717 488 LAEEWAALKLALELLEEA 505
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-512 |
4.82e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.82e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 458 CACNPLGTIPGGnpCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLdgcrPCDC 512
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-455 |
5.06e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 5.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 398 CTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLSAEDPYGC 455
Cdd:pfam00053 1 CDCNPHGSLSDT-CDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1545-1777 |
9.01e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1545 EDIRERVETL--------------SQVEVILQ--QSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVA 1608
Cdd:PRK03918 111 SSVREWVERLipyhvflnaiyirqGEIDAILEsdESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1609 AEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLER---NVEELKRKAAQNSGEAEYIEKVVYSVKQNADD 1685
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1686 VKKTLDgELDEKYKKVESLiaqktEESADARRKAELLQNEAKTLLAQANSKL----QLLEDLERKYEDnqkyLEDKAQEL 1761
Cdd:PRK03918 271 LKKEIE-ELEEKVKELKEL-----KEKAEEYIKLSEFYEEYLDELREIEKRLsrleEEINGIEERIKE----LEEKEERL 340
|
250
....*....|....*.
gi 1666305206 1762 VRLEGEVRSLLKDISE 1777
Cdd:PRK03918 341 EELKKKLKELEKRLEE 356
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1558-1768 |
1.04e-09 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 60.22 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1558 EVILQQSaadIARAELLLEEAKRAS-KSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADED--------IQGTQNLLT 1628
Cdd:COG1842 25 EKMLDQA---IRDMEEDLVEARQALaQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDlarealerKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1629 SIESETAASEETLTNASQRISKLERNVEELKRK-----AAQNSGEA-EYIEKVVYSVkqNADDVKKTLDgeldekykkve 1702
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKkdtlkARAKAAKAqEKVNEALSGI--DSDDATSALE----------- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1703 sliaqkteesaDARRKAEllQNEAKtllAQANSKLQLLEDLERKYEDnqkyLEDKAQ---ELVRLEGEV 1768
Cdd:COG1842 169 -----------RMEEKIE--EMEAR---AEAAAELAAGDSLDDELAE----LEADSEvedELAALKAKM 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1475-1782 |
1.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1475 AKQNAQDVLLKTNATKEKVDK---SNEDLRNLIKQIRNFLTEDSADLDSIEAvanevlkmEMPSTPQQLQNLT------E 1545
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKfikRTENIEELIKEKEKELEEVLREINEISS--------ELPELREELEKLEkevkelE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1546 DIRERVETLSQVEVILQQSAADIarAELLLEEAKRASKSATDVKVTADMVKEaLEEAEKAQVAAEKAIKQADEDIQGTQN 1625
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKL--EEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1626 L---LTSIESETAASEETLTNASQ---RISKLERNVEELKRKAAQNSGEAEYIEKVVySVKQNADDVKKTLDG------- 1692
Cdd:PRK03918 312 IekrLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGltpekle 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 -----------ELDEKYKKVESLIAQKTEESADaRRKA----------------ELLQNEAKTLLAQ-------ANSKLQ 1738
Cdd:PRK03918 391 keleelekakeEIEEEISKITARIGELKKEIKE-LKKAieelkkakgkcpvcgrELTEEHRKELLEEytaelkrIEKELK 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1666305206 1739 LLEDLERKYEDNQKYLE---DKAQELVRLEgEVRSLLKDISEKVAVY 1782
Cdd:PRK03918 470 EIEEKERKLRKELRELEkvlKKESELIKLK-ELAEQLKELEEKLKKY 515
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1456-1691 |
1.31e-09 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 60.76 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNF-----LTEDSAD------LD-SIEA 1523
Cdd:smart00283 39 ANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIgeivsVIDDIADqtnllaLNaAIEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 ------------VANEVlkmempstpqqlQNLTEdirervETlsqvevilQQSAADIarAELLLEEAKRASKSATDVKVT 1591
Cdd:smart00283 119 arageagrgfavVADEV------------RKLAE------RS--------AESAKEI--ESLIKEIQEETNEAVAAMEES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 ADMVKEALEEAEKAqvaaekaiKQADEDI-QGTQNLLTSIESETAASEETlTNASQRISkleRNVEELKRKAAQNSGEAE 1670
Cdd:smart00283 171 SSEVEEGVELVEET--------GDALEEIvDSVEEIADLVQEIAAATDEQ-AAGSEEVN---AAIDEIAQVTQETAAMSE 238
|
250 260
....*....|....*....|.
gi 1666305206 1671 YIEKVVYSVKQNADDVKKTLD 1691
Cdd:smart00283 239 EISAAAEELSGLAEELDELVE 259
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1216-1778 |
2.10e-09 |
|
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: 62.76 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1216 YRETVDSVEKKVNEIKDILAQSPAAE-PLKNIGILFEEAEKLTKDVTEKMAQV----EVKLTDTASQSNSTAGELGA--- 1287
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDnEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERelv 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1288 -LQAEAESLDKTVKELA-EQLEFIKNsdiQGALdsitkyfqmSLEAEK-----RVNASTTDPNST-VEQSALTRDRVEDL 1359
Cdd:TIGR00606 323 dCQRELEKLNKERRLLNqEKTELLVE---QGRL---------QLQADRhqehiRARDSLIQSLATrLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1360 MLERESPFK-EQQEEQARLLDELAGKLQSLDLSAVAQmtcgtppgADCSESECGGPNcRTDEGEKKCGGPGCGGLVTV-- 1436
Cdd:TIGR00606 391 QIKNFHTLViERQEDEAKTAAQLCADLQSKERLKQEQ--------ADEIRDEKKGLG-RTIELKKEILEKKQEELKFVik 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1437 ----AHSAWQKAMDFDRDVLSALAEVEQLSKMVS-EAKVRADEAKQNAQDVLLKTnatKEKVDKSNEDL---RNLIKQIR 1508
Cdd:TIGR00606 462 elqqLEGSSDRILELDQELRKAERELSKAEKNSLtETLKKEVKSLQNEKADLDRK---LRKLDQEMEQLnhhTTTRTQME 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1509 NfLTEDSADLDS----IEAVANEVLKMEMPSTPQQ------LQNLTEDIRERVETLSQVEVILQQSAAD----------I 1568
Cdd:TIGR00606 539 M-LTKDKMDKDEqirkIKSRHSDELTSLLGYFPNKkqledwLHSKSKEINQTRDRLAKLNKELASLEQNknhinnelesK 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1569 ARAELLLEEAKRASKSATDVKVTADMVKEALEEAEK--AQVAAEKA-----IKQADEDIQGT--------------QNLL 1627
Cdd:TIGR00606 618 EEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKqrAMLAGATAvysqfITQLTDENQSCcpvcqrvfqteaelQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1628 TSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKT---LDGELDEKYKKVESL 1704
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDiqrLKNDIEEQETLLGTI 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1705 IAQktEESADA---------RRKAELLQNEAKtlLAQANSKLQLLeDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDI 1775
Cdd:TIGR00606 778 MPE--EESAKVcltdvtimeRFQMELKDVERK--IAQQAAKLQGS-DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
...
gi 1666305206 1776 SEK 1778
Cdd:TIGR00606 853 QDQ 855
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1217-1770 |
2.17e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 62.92 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1217 RETVDSVEKKVNEIKDILAQSPA-AEPLKNIGIlfEEAEKLTKDVTEKMAQVEVKLTDTASQsnsTAGELGALQAEAESL 1295
Cdd:NF041483 469 REAVQQIEEAARTAEELLTKAKAdADELRSTAT--AESERVRTEAIERATTLRRQAEETLER---TRAEAERLRAEAEEQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1296 DKTVKELAEQLEFIKNSDIQGAL-----DSITKYFQMSLEAEKRVNASttdpnstveQSALTRDRVEDLMLERESpfkeq 1370
Cdd:NF041483 544 AEEVRAAAERAARELREETERAIaarqaEAAEELTRLHTEAEERLTAA---------EEALADARAEAERIRREA----- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1371 QEEQARLLDELAGKLQSLDLSAVAQMT-CGTPPGADCSESECGGPNC----RTD---EGEkkcggpgcgGLVTVAhsawQ 1442
Cdd:NF041483 610 AEETERLRTEAAERIRTLQAQAEQEAErLRTEAAADASAARAEGENVavrlRSEaaaEAE---------RLKSEA----Q 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1443 KAMDFDRDVLSALAE--VEQLSKMVSEAKVRADEAKQNAQDVL--LKTNATKEKvDKSNEDLRNLIKQIRNFLTEDSADL 1518
Cdd:NF041483 677 ESADRVRAEAAAAAErvGTEAAEALAAAQEEAARRRREAEETLgsARAEADQER-ERAREQSEELLASARKRVEEAQAEA 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1519 DSIEAVANEvLKMEMPSTPQQlqnLTEDIRERVETL---SQVEVILQQSAADIArAELLLEEAK---------------R 1580
Cdd:NF041483 756 QRLVEEADR-RATELVSAAEQ---TAQQVRDSVAGLqeqAEEEIAGLRSAAEHA-AERTRTEAQeeadrvrsdayaereR 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 ASKSATDVKvtadmvKEALEEAEKAQVAAEKAIKQADEDIQgtqnLLTSIESETAasEETLTNASQRISKLERNV----- 1655
Cdd:NF041483 831 ASEDANRLR------REAQEETEAAKALAERTVSEAIAEAE----RLRSDASEYA--QRVRTEASDTLASAEQDAartra 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 ---EELKRKAAQNSGEAE-YIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEES----ADARRKAELLQNEAK 1727
Cdd:NF041483 899 darEDANRIRSDAAAQADrLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAeqliAEATGEAERLRAEAA 978
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1666305206 1728 TLLAQANsklqllEDLERKYEDNQKYLEDKAQELVRLEGEVRS 1770
Cdd:NF041483 979 ETVGSAQ------QHAERIRTEAERVKAEAAAEAERLRTEARE 1015
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1581-1770 |
2.79e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.38 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 ASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKR 1660
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1661 KAAQNSGEAEYIEKV------------VYSVKQNADDVKKTLDgELDEKYKKVESLIAQKTEESADARRKAELLQNEAKT 1728
Cdd:COG3883 94 ALYRSGGSVSYLDVLlgsesfsdfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1666305206 1729 LLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRS 1770
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1485-1696 |
3.02e-09 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 59.27 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1485 KTNATKEKVDKSNEDLRNLIKQIRNflTEDSAdldsieavanEVLKMEMPSTPQQLQNLTEDIR---ERVET----LSQV 1557
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEE--AEKRA----------EKAEAEVAALNRRIQLLEEELErteERLAEalekLEEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1558 E-----------VILQQSAADIARAELL---LEEAKRASKSA----TDVKVTADMVKEALEEAEKAQVAAEKAIKQADED 1619
Cdd:pfam00261 70 EkaadesergrkVLENRALKDEEKMEILeaqLKEAKEIAEEAdrkyEEVARKLVVVEGDLERAEERAELAESKIVELEEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1620 IQGTQNLLTSIE-SETAASE-------------ETLTNASQRISKLERNVEELKRkaaqnsgEAEYIEKVVYSVKQNADD 1685
Cdd:pfam00261 150 LKVVGNNLKSLEaSEEKASEredkyeeqirfltEKLKEAETRAEFAERSVQKLEK-------EVDRLEDELEAEKEKYKA 222
|
250
....*....|.
gi 1666305206 1686 VKKTLDGELDE 1696
Cdd:pfam00261 223 ISEELDQTLAE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1456-1674 |
3.49e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIrNFLTEDSADLDSIEAVANEVLKmemps 1535
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAELE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1536 tpQQLQNLTEDIRE--RVETLSQVEVIL-QQSAADIARAELLLEEAKRASKS-ATDVKVTADMVKEALEEAEKAQVAAEK 1611
Cdd:COG4942 101 --AQKEELAELLRAlyRLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1612 AIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEK 1674
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
509-548 |
4.56e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1666305206 509 PCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
866-911 |
4.74e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1666305206 866 PCQCNGHA---LDCDTVTGECLsCQDYTTGHNCERCLAGYYGDPIIGSG 911
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1763 |
4.92e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 61.77 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDlrnlikQIRNFLTEDSA-DLDSIEAVANEVLKM---EMP 1534
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE------KARTVAAEDTAaQLAKAARTAEEVLTKaseDAK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1535 STPQQLQNLTEDIRERVETLSQVeviLQQSAADIA--------------RAEL--LLEEAKRASKSATDVKVtadmvkEA 1598
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADR---LRGEAADQAeqlkgaakddtkeyRAKTveLQEEARRLRGEAEQLRA------EA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1599 LEEAEKAQVAAEK-AIKQADEDIQGTQNLLTSIESE--------TAASEETLTNASQRISKLERNVEE-LKR---KAAQN 1665
Cdd:NF041483 457 VAEGERIRGEARReAVQQIEEAARTAEELLTKAKADadelrstaTAESERVRTEAIERATTLRRQAEEtLERtraEAERL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1666 SGEAEyiekvvysvkQNADDVKKTLDGELDEKYKKVESLIAQKTEESADarrkaEL--LQNEAKTLLAQANSKL----QL 1739
Cdd:NF041483 537 RAEAE----------EQAEEVRAAAERAARELREETERAIAARQAEAAE-----ELtrLHTEAEERLTAAEEALadarAE 601
|
330 340
....*....|....*....|....
gi 1666305206 1740 LEDLERKYEDNQKYLEDKAQELVR 1763
Cdd:NF041483 602 AERIRREAAEETERLRTEAAERIR 625
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1607-1780 |
5.70e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1607 VAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKvvysvkqnaddv 1686
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1687 kktldgELDEKYKKVESLIA--QKTEES-------------ADARRKAELLQneakTLLAQANSKLQLLEDLERKYEDNQ 1751
Cdd:COG3883 80 ------EIEERREELGERARalYRSGGSvsyldvllgsesfSDFLDRLSALS----KIADADADLLEELKADKAELEAKK 149
|
170 180
....*....|....*....|....*....
gi 1666305206 1752 KYLEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQA 178
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1590-1780 |
6.33e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1590 VTAD----MVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELK------ 1659
Cdd:COG3883 12 AFADpqiqAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelger 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1660 -RKAAQNSGEAEYIEKVVYSvkQNADDVkktldgeldekykkVESLIAQKTEESADARrkaelLQNEAKTLLAQANSKLQ 1738
Cdd:COG3883 92 aRALYRSGGSVSYLDVLLGS--ESFSDF--------------LDRLSALSKIADADAD-----LLEELKADKAELEAKKA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1666305206 1739 LLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
867-914 |
7.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 867 CQCNGHA---LDCDTVTGECLsCQDYTTGHNCERCLAGYYGDPiIGSGDHC 914
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1187-1777 |
8.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1187 DAIIGELTNRTHKfLEK--AKALKisgvigpYRETVDSVEKK-----VNEIKDILAQspaaepLKNIGILFEEAEKLTKD 1259
Cdd:COG1196 192 EDILGELERQLEP-LERqaEKAER-------YRELKEELKELeaellLLKLRELEAE------LEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1260 VTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKNsDIQGALDSITKyfqmsLEAEKRVNAST 1339
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEE-----LEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1340 TDpnSTVEQSALTRDRVEDLMLERESpFKEQQEEQARLLDELAGKLQSLDLSAVAQmtcgtppgadcsesecggpncRTD 1419
Cdd:COG1196 332 LE--ELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEEL---------------------AEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1420 EGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNED 1499
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1500 LRNLIKQIRNFLTEDSADLDSIEAVANEVLKME-------MPSTPQQLQNLTEDIRERVETLSQVEV------------- 1559
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflEGVKAALLLAGLRGLAGAVAVLIGVEAayeaaleaalaaa 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1560 ILQQSAADIARAELLLEEAKRASKS-ATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQ--GTQNLLTSIESETAA 1636
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREadARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1637 SEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADAR 1716
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 1717 RKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVR----------LEGEVRSLLKDISE 1777
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdleeLERELERLEREIEA 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1451-1686 |
8.61e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1451 VLSALAEVEQlskmvSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIrnflTEDSADLDSIEAvanEVLK 1530
Cdd:COG3883 9 PTPAFADPQI-----QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKLQA---EIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1531 MEmpstpQQLQNLTEDIRERV-------ETLSQVEVILQ-QSAAD-IARAELLLEEAKRASKSATDVKVTADMVKEALEE 1601
Cdd:COG3883 77 AE-----AEIEERREELGERAralyrsgGSVSYLDVLLGsESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 AEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQ 1681
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 1666305206 1682 NADDV 1686
Cdd:COG3883 232 AAAAA 236
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
510-548 |
9.68e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 9.68e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1666305206 510 CDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1028-1081 |
9.87e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.74 E-value: 9.87e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1028 CVCNYLGTVkehcngsDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQLAS-GTGC 1081
Cdd:cd00055 2 CDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1028-1081 |
1.02e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.70 E-value: 1.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1028 CVCNYLGTVkehcngsDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQlASGTGC 1081
Cdd:smart00180 1 CDCDPGGSA-------SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1588-1773 |
1.39e-08 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 57.35 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1588 VKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKR--KAAQN 1665
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrKVLEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1666 SGEA--EYIEKVVYSVKQnaddvKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTL---LAQANSKLQLL 1740
Cdd:pfam00261 86 RALKdeEKMEILEAQLKE-----AKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELeeeLKVVGNNLKSL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1666305206 1741 E-------DLERKYEDNQKYLEDKAQELV-RLEGEVRSLLK 1773
Cdd:pfam00261 161 EaseekasEREDKYEEQIRFLTEKLKEAEtRAEFAERSVQK 201
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-501 |
1.46e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 458 CACNPLGTIpgGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLS 501
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1187-1780 |
1.65e-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: 59.70 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1187 DAIIGELTNRTHKF-LEKAKALKisgvigpYRETVDSVEK-----KVNEIKDILAQSPAAEplKNIGILFEEAEKLTKDV 1260
Cdd:TIGR02169 190 DLIIDEKRQQLERLrREREKAER-------YQALLKEKREyegyeLLKEKEALERQKEAIE--RQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1261 TEK---MAQVEVKLTDTASQSNSTAGE--------LGALQAEAESLDKTVKELAEQLEfiknsdiqgaldsitkyfqmsl 1329
Cdd:TIGR02169 261 SELekrLEEIEQLLEELNKKIKDLGEEeqlrvkekIGELEAEIASLERSIAEKERELE---------------------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1330 EAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLlDELAGKLQSLDLSAVAqmtcgtppgadcSES 1409
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAE------------TRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1410 ECGGPNCRTDE--GEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSkmvSEAKVRADEAKQNAQDvLLKTN 1487
Cdd:TIGR02169 386 ELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIKKQEWK-LEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1488 ATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQnLTEDIRERVETLSQ----------- 1556
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV-LKASIQGVHGTVAQlgsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1557 VEV--------ILQQSAADIARAELLLEEAK--RA---------------SKSATD--VKVTADMVK------------- 1596
Cdd:TIGR02169 541 IEVaagnrlnnVVVEDDAVAKEAIELLKRRKagRAtflplnkmrderrdlSILSEDgvIGFAVDLVEfdpkyepafkyvf 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1597 ------EALEEA-----------------EKAQV---------------AAEKA-IKQADEDIQGTQNLL-------TSI 1630
Cdd:TIGR02169 621 gdtlvvEDIEAArrlmgkyrmvtlegelfEKSGAmtggsraprggilfsRSEPAeLQRLRERLEGLKRELsslqselRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1631 ESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQ---NADDVKKTLDGELDEKYKKVESLIAQ 1707
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeieNVKSELKELEARIEELEEDLHKLEEA 780
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1708 KTE-ESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQ---KYLEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:TIGR02169 781 LNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1288-1777 |
1.75e-08 |
|
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: 59.80 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1288 LQAEAESLDKtVKELAEQLEfiknsdiqGALDSITKYFQmSLEAEKrvnasttdpnstveqSALTrdrvEDLMLERESpF 1367
Cdd:pfam01576 7 MQAKEEELQK-VKERQQKAE--------SELKELEKKHQ-QLCEEK---------------NALQ----EQLQAETEL-C 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1368 KEQQEEQARLldelAGKLQSLDLsAVAQMtcgtppgadcsESecggpncRTDEGEKKCGGPgcgglvtvaHSAWQKAMDF 1447
Cdd:pfam01576 57 AEAEEMRARL----AARKQELEE-ILHEL-----------ES-------RLEEEEERSQQL---------QNEKKKMQQH 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1448 DRDVLSALAEVE------QLSKMVSEAKVRADEAkqnaqDVLLKTNAtKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSI 1521
Cdd:pfam01576 105 IQDLEEQLDEEEaarqklQLEKVTTEAKIKKLEE-----DILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1522 EAVAN----------------EVLKMEMPSTPQQLQNLTEDIRERVETL-SQVEVILQQSA-------ADIARAElllEE 1577
Cdd:pfam01576 179 SKLKNkheamisdleerlkkeEKGRQELEKAKRKLEGESTDLQEQIAELqAQIAELRAQLAkkeeelqAALARLE---EE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1578 AKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQA---DEDIQGTQNLLTSIESETAASEETLTNASQRISKLERN 1654
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRrdlGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1655 VEE-----------LKRKAAQNSGE-AEYIEkVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTeESADARRKAEll 1722
Cdd:pfam01576 336 LEEetrsheaqlqeMRQKHTQALEElTEQLE-QAKRNKANLEKAKQALESENAELQAELRTLQQAKQ-DSEHKRKKLE-- 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1723 qneaktllAQansklqlLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:pfam01576 412 --------GQ-------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1251-1755 |
2.05e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.45 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVtekMAQVEvKLTDTASQSNSTAG-ELGALQAEAEsldKTVKELAEQLEFIKnSDiqgaldsitkyfqmSL 1329
Cdd:NF041483 815 EEADRVRSDA---YAERE-RASEDANRLRREAQeETEAAKALAE---RTVSEAIAEAERLR-SD--------------AS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1330 EAEKRVNASTTDPNSTVEQSAlTRDRVEdlmlerespfkeQQEEQARLLDELAGKLQSLdlsaVAQMTcgtppgadcSES 1409
Cdd:NF041483 873 EYAQRVRTEASDTLASAEQDA-ARTRAD------------AREDANRIRSDAAAQADRL----IGEAT---------SEA 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1410 ECGGPNCRTdEGEKKCGGPGCGGLVTVAHSAWQKamdfDRDVLSALAEVEQLSkmvSEAKVRADEAKQNAQDVLLKTNAT 1489
Cdd:NF041483 927 ERLTAEARA-EAERLRDEARAEAERVRADAAAQA----EQLIAEATGEAERLR---AEAAETVGSAQQHAERIRTEAERV 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KEKVDKSNEDLRNLIKqirnflTEDSADLDSIEAVANevlkmempstpqqlqnltediRERVETLSQVEVILQQSAADia 1569
Cdd:NF041483 999 KAEAAAEAERLRTEAR------EEADRTLDEARKDAN---------------------KRRSEAAEQADTLITEAAAE-- 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 rAELLLEEAK-RASKSATDVKVTAD-MVKEALEEAEKAQVAA--------EKAIKQADEDIQGTQNLLTSIESETaasEE 1639
Cdd:NF041483 1050 -ADQLTAKAQeEALRTTTEAEAQADtMVGAARKEAERIVAEAtvegnslvEKARTDADELLVGARRDATAIRERA---EE 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1640 TLTnasqrisKLERNVEELKRKAAQNSGEA-----EYIEKVVYSVKQN---ADDVKKTLDGELDEK--------YKKVES 1703
Cdd:NF041483 1126 LRD-------RITGEIEELHERARRESAEQmksagERCDALVKAAEEQlaeAEAKAKELVSDANSEaskvriaaVKKAEG 1198
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1704 LIAQKTEESADARRKAELLQN----EAKTLLAQANSKLQLL----EDLERKYEDNQKYLE 1755
Cdd:NF041483 1199 LLKEAEQKKAELVREAEKIKAeaeaEAKRTVEEGKRELDVLvrrrEDINAEISRVQDVLE 1258
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1454-1759 |
2.07e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1454 ALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNF------LTEDSADLDS-IEAVAN 1526
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEeLEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1527 EV--LKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARaellLEEAKRASKSATDVKVTADMVKEALEEAEK 1604
Cdd:COG4372 123 ERqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA----LEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1605 AQVAAE---KAIKQADEDIQGTQNLLTSIESETAASEETLTNAsqriskLERNVEELKRKAAQNSGEAEYIEKVVYSVKQ 1681
Cdd:COG4372 199 EEELAEaekLIESLPRELAEELLEAKDSLEAKLGLALSALLDA------LELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1682 NADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQ 1759
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1470-1735 |
2.15e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1470 VRADEAKQNAQDVLlktNATKEKVDKSNEDLRNLIKQIrnflTEDSADLDSIEAvANEVLKMEMPSTPQQLQNLTEDIRE 1549
Cdd:COG3883 12 AFADPQIQAKQKEL---SELQAELEAAQAELDALQAEL----EELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1550 RVETLSQVEVILQQSAADIARAELLLEeakraSKSATDvkvtadmvkeALEEAEkaqvAAEKAIKQADEDIQGTQNLLTS 1629
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLG-----SESFSD----------FLDRLS----ALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1630 IESETAASEETLTNASQRISKLERNVEELKRKAAQnsgeaeyiekvvysvkqnADDVKKTLDGELDEKYKKVESLIAQKT 1709
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAE------------------QEALLAQLSAEEAAAEAQLAELEAELA 206
|
250 260
....*....|....*....|....*.
gi 1666305206 1710 EESADARRKAELLQNEAKTLLAQANS 1735
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-456 |
4.21e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 4.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 397 PCTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLsAEDPYGCK 456
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGT--------GQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1471-1767 |
4.40e-08 |
|
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: 58.26 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1471 RADEAKQNAQDVLLKTnatKEKVDKSNEDLRNLIKQIRNFLTEDSAdldsieavANEVLKMEmpstpQQLQNLTEDIRER 1550
Cdd:pfam01576 2 RQEEEMQAKEEELQKV---KERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAE-----TELCAEAEEMRAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1551 VETLSQ-VEVILQQSAADIA----RAELLLEEAKRASKSATDVKvtadmvkEALEEAEKA-------QVAAEKAIKQADE 1618
Cdd:pfam01576 66 LAARKQeLEEILHELESRLEeeeeRSQQLQNEKKKMQQHIQDLE-------EQLDEEEAArqklqleKVTTEAKIKKLEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1619 DIQGTQNLLTSIESETAASEETLTNASQRISKLE---RNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELD 1695
Cdd:pfam01576 139 DILLLEDQNSKLSKERKLLEERISEFTSNLAEEEekaKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1696 EKYKKVESLIAQKTEESADARRKAELLQ---------NEAKTLLAQANSKLQ-----LLEDLERK---YEDNQKYLEDKA 1758
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQaalarleeeTAQKNNALKKIRELEaqiseLQEDLESEraaRNKAEKQRRDLG 298
|
....*....
gi 1666305206 1759 QELVRLEGE 1767
Cdd:pfam01576 299 EELEALKTE 307
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1538-1777 |
4.42e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERV----ETLSQVEvILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAI 1613
Cdd:COG4913 204 KPIGDLDDFVREYMleepDTFEAAD-ALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1614 KQADEDIQGT-QNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEaeyiekvvysvkqnaddvkktldg 1692
Cdd:COG4913 283 LWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------------------------ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ELDEkykkVESLIAQKTEESADARRKAELLQNEAKTL----------LAQANSKL-QLLEDLERKYEDNQKYLEDKAQEL 1761
Cdd:COG4913 339 RLEQ----LEREIERLERELEERERRRARLEALLAALglplpasaeeFAALRAEAaALLEALEEELEALEEALAEAEAAL 414
|
250
....*....|....*.
gi 1666305206 1762 VRLEGEVRSLLKDISE 1777
Cdd:COG4913 415 RDLRRELRELEAEIAS 430
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1449-1691 |
4.64e-08 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 56.90 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RDVLSALAEV-----EQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNL----IKQIRNFLTEDSADLD 1519
Cdd:pfam09311 22 RDQVKKLQEMlrqanDQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLLDELqqafSQAKRNFQDQLAVLMD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1520 SIEAVANEVL-----------------------KMEMPSTPQQLQNLTEDIRER-VETLSQVEVILQQSAADIA--RAEL 1573
Cdd:pfam09311 102 SREQVSDELVrlqkdneslqgkhslhvslqqaeKFDMPDTVQELQELVLKYREElIEVRTAADHMEEKLKAEILflKEQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1574 LLEEAkrasksatdvkvtadmVKEALEEAEKAQvaaekaIKQADEDIQGTQNL---LTSIESETAASEETLTNASQRISK 1650
Cdd:pfam09311 182 QAEQC----------------LKENLEETLQAE------IENCKEEIASISSLkveLERIKAEKEQLENGLTEKIRQLED 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1666305206 1651 LERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLD 1691
Cdd:pfam09311 240 LQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELD 280
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1251-1771 |
4.77e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 58.30 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVTEKM----AQVEV---KLTDTASQSNSTAgelgalQAEAESLDKTVK-ELAEQLEFIKnSDIQGALDSIT 1322
Cdd:NF041483 611 EETERLRTEAAERIrtlqAQAEQeaeRLRTEAAADASAA------RAEGENVAVRLRsEAAAEAERLK-SEAQESADRVR 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1323 KYFQMSLEaekRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLldelagklQSLDLSAVAQMtcgtpp 1402
Cdd:NF041483 684 AEAAAAAE---RVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERARE--------QSEELLASARK------ 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1403 gadcsesecggpncRTDEGEKKCG------GPGCGGLVTVAHSAWQKAmdfdRDVLSALAEV--EQLSKMVSEAKVRADE 1474
Cdd:NF041483 747 --------------RVEEAQAEAQrlveeaDRRATELVSAAEQTAQQV----RDSVAGLQEQaeEEIAGLRSAAEHAAER 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1475 AKQNAQDVL--LKTNATKEKvDKSNEDLRnlikQIRNFLTEDS------ADLDSIEAVAN-EVLKMEMPSTPQQLQNLTE 1545
Cdd:NF041483 809 TRTEAQEEAdrVRSDAYAER-ERASEDAN----RLRREAQEETeaakalAERTVSEAIAEaERLRSDASEYAQRVRTEAS 883
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1546 DI--------------------RERVETLSQVEVILQQSAADIAR--------AELLLEEA-KRASKSATDVKVTAD-MV 1595
Cdd:NF041483 884 DTlasaeqdaartradaredanRIRSDAAAQADRLIGEATSEAERltaearaeAERLRDEArAEAERVRADAAAQAEqLI 963
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1596 KEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQriSKLERNVEELKRKAAQNSGE-AEYIEK 1674
Cdd:NF041483 964 AEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAR--EEADRTLDEARKDANKRRSEaAEQADT 1041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1675 VVYSVKQNADdvkkTLDGELDEKYKKVesliAQKTEESAD-----ARRKAELLQNEA----KTLLAQANSKL-QLLEDLE 1744
Cdd:NF041483 1042 LITEAAAEAD----QLTAKAQEEALRT----TTEAEAQADtmvgaARKEAERIVAEAtvegNSLVEKARTDAdELLVGAR 1113
|
570 580
....*....|....*....|....*...
gi 1666305206 1745 RkyedNQKYLEDKAQEL-VRLEGEVRSL 1771
Cdd:NF041483 1114 R----DATAIRERAEELrDRITGEIEEL 1137
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1497-1701 |
4.86e-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: 55.70 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1497 NEDLRNLIK-QirnflTEDSAdLDSIEAVANEVlkmempstPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLL 1575
Cdd:COG1579 3 PEDLRALLDlQ-----ELDSE-LDRLEHRLKEL--------PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1576 EEA----KRASK---SATDVKVTADMVKEaLEEAEKAQVAAEKAIKQADEDIqgtqnlltsiesetAASEETLTNASQRI 1648
Cdd:COG1579 69 EEVeariKKYEEqlgNVRNNKEYEALQKE-IESLKRRISDLEDEILELMERI--------------EELEEELAELEAEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1649 SKLERNVEELKrkaAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKV 1701
Cdd:COG1579 134 AELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-1777 |
6.08e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1450 DVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNAT-KEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEv 1528
Cdd:PRK02224 156 DDLLQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 lkmempsTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVT-ADMVKEALEEAEkaqv 1607
Cdd:PRK02224 235 -------TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEAG---- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1608 aaekaikqadediqgtqnlLTSIESETAaseetltnaSQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVK 1687
Cdd:PRK02224 304 -------------------LDDADAEAV---------EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1688 KTLDgELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQansklqlLEDLERKYEDNQKYLEDKAQELVRLEGE 1767
Cdd:PRK02224 356 ERAE-ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER-------FGDAPVDLGNAEDFLEELREERDELRER 427
|
330
....*....|
gi 1666305206 1768 VRSLLKDISE 1777
Cdd:PRK02224 428 EAELEATLRT 437
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1484-1746 |
6.32e-08 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 56.74 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1484 LKTNATKEkvDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKMEmpstpqqlQNLTEDIRERVETLSQVEViLQQ 1563
Cdd:pfam15905 61 LKKKSQKN--LKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVE--------AKLNAAVREKTSLSASVAS-LEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1564 SAADIARA-ELLLEEA------KRAS---------KSATDVKVTADMVKEalEEAEKAQVAAEKAIKQADEDIQGTQNLL 1627
Cdd:pfam15905 130 QLLELTRVnELLKAKFsedgtqKKMSslsmelmklRNKLEAKMKEVMAKQ--EGMEGKLQVTQKNLEHSKGKVAQLEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1628 TSIES---ETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAE----YIEKVVYSVKQNADDVKKTLdGELDEKYKK 1700
Cdd:pfam15905 208 VSTEKekiEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKekndEIESLKQSLEEKEQELSKQI-KDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1666305206 1701 VESliaQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERK 1746
Cdd:pfam15905 287 LES---EKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1225-1760 |
8.50e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1225 KKVNEIKDILAQSPAAEPLKNIGilfEEAEK----LTKDVTEKMAQVEVKLTDT--------ASQSNSTAGELGALQAE- 1291
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKA---EEAKKkadaAKKKAEEAKKAAEAAKAEAeaaadeaeAAEEKAEAAEKKKEEAKk 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1292 -AESLDKTVKEL--AEQLEFIKNSDIQGAlDSITKYfqmslEAEKRVNASTTDPNSTVEQSALTRDRVEDlmlERESPFK 1368
Cdd:PTZ00121 1379 kADAAKKKAEEKkkADEAKKKAEEDKKKA-DELKKA-----AAAKKKADEAKKKAEEKKKADEAKKKAEE---AKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1369 EQQEEQARLLDELAGKLQSLDLSAVAQMTCGTPPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAwQKAMDFD 1448
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAK 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RdvLSALAEVEQLSKmvSEAKVRADEAKQ-----NAQDVLLKTNATKEKVDKsNEDLR--NLIKQIRNFLTEDSADLDSI 1521
Cdd:PTZ00121 1529 K--AEEAKKADEAKK--AEEKKKADELKKaeelkKAEEKKKAEEAKKAEEDK-NMALRkaEEAKKAEEARIEEVMKLYEE 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1522 EavanEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEE 1601
Cdd:PTZ00121 1604 E----KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 AEKAQ---VAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLE----------RNVEELKRkaaqNSGE 1668
Cdd:PTZ00121 1680 AKKAEedeKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEeakkeaeedkKKAEEAKK----DEEE 1755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1669 AEYIEKVVYSVKQNADDVKKTLDG----ELDEKYKKVESLIAQKTEESAD-------ARRKAELLQNEAKTLLAQANSKL 1737
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAvieeELDEEDEKRRMEVDKKIKDIFDnfaniieGGKEGNLVINDSKEMEDSAIKEV 1835
|
570 580
....*....|....*....|....
gi 1666305206 1738 QLLEDLERKYEDN-QKYLEDKAQE 1760
Cdd:PTZ00121 1836 ADSKNMQLEEADAfEKHKFNKNNE 1859
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1206-1621 |
1.17e-07 |
|
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: 56.50 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1206 ALKISGVIGPYRETVDSVEKKVNeIKDILAQSPAAEplknigILFEEAEKLTKDVT---EKMAQVEVKLTDTASQSN--- 1279
Cdd:COG5185 194 ELKKAEPSGTVNSIKESETGNLG-SESTLLEKAKEI------INIEEALKGFQDPEselEDLAQTSDKLEKLVEQNTdlr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1280 -----STAGELGALQAEAESLDKTVKELAEQL-EFIKNSDIQGALDSITKYFQmSLEAEKRVnasttdpnstveqsaltr 1353
Cdd:COG5185 267 leklgENAESSKRLNENANNLIKQFENTKEKIaEYTKSIDIKKATESLEEQLA-AAEAEQEL------------------ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1354 drvEDLMLERESPFKEQQEEQARLLDELAGKLQSLDLSAvaqmtcgtppgadcsESECGGPNCRTDEgekkcggpgcggl 1433
Cdd:COG5185 328 ---EESKRETETGIQNLTAEIEQGQESLTENLEAIKEEI---------------ENIVGEVELSKSS------------- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1434 vtvahsawqkamdfdrdvlsalAEVEQLSKMVSEAKVRADEAKQNA----QDVLLKTNATKEKVDKSNEDLRNLIKQIRN 1509
Cdd:COG5185 377 ----------------------EELDSFKDTIESTKESLDEIPQNQrgyaQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1510 FLTEDSADLDSIEAVANEVLKMEMPSTPQQLQN----LTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSA 1585
Cdd:COG5185 435 SNEEVSKLLNELISELNKVMREADEESQSRLEEaydeINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
410 420 430
....*....|....*....|....*....|....*.
gi 1666305206 1586 TDVKVTADMVKEALEEaekaqVAAEKAIKQADEDIQ 1621
Cdd:COG5185 515 VRSKLDQVAESLKDFM-----RARGYAHILALENLI 545
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1224-1770 |
1.66e-07 |
|
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: 56.29 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1224 EKKVNEIKD----ILAQSPAAEPLKNigiLFEEAEKLtKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTV 1299
Cdd:pfam05557 17 EKKQMELEHkrarIELEKKASALKRQ---LDRESDRN-QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1300 KELAEQLEfiKNSDIQGAL-DSITKYFQMSLEAEkrvnasttdpnstveqSALTRDRVEdlmLERespFKEQQEEQARLL 1378
Cdd:pfam05557 93 NEKESQLA--DAREVISCLkNELSELRRQIQRAE----------------LELQSTNSE---LEE---LQERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1379 DELAGKLQSLdlsavaQMTCgtppgadcseSECGGPNCRTDEGEKKCGGPGCGGLVTvahsawqKAMDfdrdvlsalAEV 1458
Cdd:pfam05557 149 SEAEQLRQNL------EKQQ----------SSLAEAEQRIKELEFEIQSQEQDSEIV-------KNSK---------SEL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKQnaqdvLLKTNATKEKVDKSNEDLRNLIKQIRNFlTEDSADLDsieaVANEVLKMEMPSTPQ 1538
Cdd:pfam05557 197 ARIPELEKELERLREHNKH-----LNENIENKLLLKEEVEDLKRKLEREEKY-REEAATLE----LEKEKLEQELQSWVK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1539 QLQN--LT----EDIRERVETLSQVEVILQQSAADI---ARAE-----LLLEEAKRASKSATDVK--------------- 1589
Cdd:pfam05557 267 LAQDtgLNlrspEDLSRRIEQLQQREIVLKEENSSLtssARQLekarrELEQELAQYLKKIEDLNkklkrhkalvrrlqr 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1590 ----VTA--DMVKEALEEAEKAQVAAE------KAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEE 1657
Cdd:pfam05557 347 rvllLTKerDGYRAILESYDKELTMSNyspqllERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1658 LKRKAAQNsgEAEYIEKVVYSVKQNADDVKKTLDgELDEKYKKVESLIAQKT-----------------EESADARR-KA 1719
Cdd:pfam05557 427 LRQQESLA--DPSYSKEEVDSLRRKLETLELERQ-RLREQKNELEMELERRClqgdydpkktkvlhlsmNPAAEAYQqRK 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 1720 ELLQneaktLLAQANSKLQ-LLEDLERKYED----NQKYLEDKAQELVRLEGEVRS 1770
Cdd:pfam05557 504 NQLE-----KLQAEIERLKrLLKKLEDDLEQvlrlPETTSTMNFKEVLDLRKELES 554
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1452-1750 |
1.82e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1452 LSALAE-----VEQLSKMVSEAKVRADEAKQNAQDVllktNATKEKVDKSNEDLRNLIKQIRNF------LTEDSADLDS 1520
Cdd:COG1340 38 LKELAEkrdelNAQVKELREEAQELREKRDELNEKV----KELKEERDELNEKLNELREELDELrkelaeLNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1521 IEAVANEVLKMempstpQQLQNLTEDiRERvetlsqvEVILQqsaadIARAELLLEEAKRASKSATDvkvtadmVKEALE 1600
Cdd:COG1340 114 LRKEIERLEWR------QQTEVLSPE-EEK-------ELVEK-----IKELEKELEKAKKALEKNEK-------LKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1601 EAEKAQVAAEKAIKQadediqgtqnlltsiesetaaseetLTNASQRISKLERNVEELKRKAAQNSGEA-EYIEKVVySV 1679
Cdd:COG1340 168 ELKELRKEAEEIHKK-------------------------IKELAEEAQELHEEMIELYKEADELRKEAdELHKEIV-EA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1680 KQNADDVKKtldgELDEKYKKV----ESLIAQKTEESADARRKA-ELLQNEAKTLLAQANSKLQL-LEDLERKYEDN 1750
Cdd:COG1340 222 QEKADELHE----EIIELQKELrelrKELKKLRKKQRALKREKEkEELEEKAEEIFEKLKKGEKLtTEELKLLQKSG 294
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1190-1618 |
1.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1190 IGELTNRTHKFLEKAKALKIsgvigpYRETVDSVEKKVNEIKDILAQspaAEPLKNIGILFEEAEKLTKDVTEKMAQVEv 1269
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEE------LEEELEELEAELEELREELEK---LEKLLQLLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1270 KLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKNSDIQGALDSITkyfqmslEAEKRVNASTTDPNSTVEQS 1349
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE-------ELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1350 ALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQSLDLSAVAQM-TCGTPPG---------ADCSESECGGPNCRTD 1419
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLsLILTIAGvlflvlgllALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1420 EGEKKCGGPGCGGLVTVAHSAWQKAMDFDRD-----VLSALAEVEQLSKMVSEA-----KVRADEAKQNAQDVLLKTNAT 1489
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDlspeeLLELLDRIEELQELLREAeeleeELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KE-----KVDKSNE--DLRNLIKQIRNFLTEDSADLDSIEAVAN-EVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVIL 1561
Cdd:COG4717 383 DEeelraALEQAEEyqELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1562 QQ--SAADIARAELLLEEAKRASKSATD----VKVTADMVKEALEEAEKAQVAaeKAIKQADE 1618
Cdd:COG4717 463 EQleEDGELAELLQELEELKAELRELAEewaaLKLALELLEEAREEYREERLP--PVLERASE 523
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1020 |
1.89e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.27 E-value: 1.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1666305206 976 CQCHHNIDTTDPeaCDKETGRCLkCLYHTEGDHCQLCQYGYYGDA 1020
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1538-1780 |
1.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLSQVEVILQQSAA----------------DIARAELLLE--EAKRASKSATDVKVTAdmVKEAL 1599
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEREIAelEAELERLDASSDDLAA--LEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1600 EEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLER-NVEELKRKAAQnsgeaeyiEKVVYS 1678
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRaLLEERFAAALG--------DAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1679 VKQNADDVKKTLDGELDEKYKKVESLIAQkteesadARRKAELLQNEAKTLLAQANSKLQLL-----EDLERKYEDNQKY 1753
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRA-------FNREWPAETADLDADLESLPEYLALLdrleeDGLPEYEERFKEL 839
|
250 260
....*....|....*....|....*...
gi 1666305206 1754 LEDKA-QELVRLEGEVRSLLKDISEKVA 1780
Cdd:COG4913 840 LNENSiEFVADLLSKLRRAIREIKERID 867
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1453-1661 |
2.55e-07 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 53.83 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNA-------TKEKVDKSNEDLRNLIKQIRNfLTEDSADLD------ 1519
Cdd:smart00283 22 ELAERMEELSASIEEVAANADEIAATAQSAAEAAEEgreavedAITAMDQIREVVEEAVSAVEE-LEESSDEIGeivsvi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1520 --------------SIEA------------VANEVLKMEmpstpQQLQNLTEDIRERVETL----SQVEVILQQSAADIA 1569
Cdd:smart00283 101 ddiadqtnllalnaAIEAarageagrgfavVADEVRKLA-----ERSAESAKEIESLIKEIqeetNEAVAAMEESSSEVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 RAELLLEEAKRASKSATD-VKVTADMVKE---ALEEaekaQVAAEKAIKQADEDIqgtqnllTSIESETAASEETLTNAS 1645
Cdd:smart00283 176 EGVELVEETGDALEEIVDsVEEIADLVQEiaaATDE----QAAGSEEVNAAIDEI-------AQVTQETAAMSEEISAAA 244
|
250
....*....|....*.
gi 1666305206 1646 QRISKLERNVEELKRK 1661
Cdd:smart00283 245 EELSGLAEELDELVER 260
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1192-1761 |
3.10e-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: 55.51 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1192 ELTNRTHKfLEKAKALKisgvigpyRETVDSVEKKVNEIKDI-LAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVK 1270
Cdd:pfam15921 146 QLQNTVHE-LEAAKCLK--------EDMLEDSNTQIEQLRKMmLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1271 ltdtaSQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKnSDIQGALDSITKYFQMSLEA-----EKRVNASTTDPNST 1345
Cdd:pfam15921 217 -----SLGSAISKILRELDTEISYLKGRIFPVEDQLEALK-SESQNKIELLLQQHQDRIEQlisehEVEITGLTEKASSA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1346 VEQSALTRDRVEDLmlerespfkeqqEEQARLLDEL-AGKLQSLDlSAVAQMTcgtppgADCSESEcggpncRTDEGEKK 1424
Cdd:pfam15921 291 RSQANSIQSQLEII------------QEQARNQNSMyMRQLSDLE-STVSQLR------SELREAK------RMYEDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1425 CGGPGcgglVTVAHSAWQKAMDfDRDVLSALAEV--EQLSKMVSEAKVRADE----AKQNAQ--DVLLKTNAT----KEK 1492
Cdd:pfam15921 346 ELEKQ----LVLANSELTEART-ERDQFSQESGNldDQLQKLLADLHKREKElsleKEQNKRlwDRDTGNSITidhlRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1493 VDKSNEDLRNLIKQIRNFLTEDSADLDSIEAV---ANEVLKmEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIA 1569
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAiqgKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 RAELLLEEAKRASKsATDVKVTA--DMVKEALEEAEKaqvaaekaIKQADEDIQGTQNLLTSIESETAASEETLTNASQR 1647
Cdd:pfam15921 500 DLTASLQEKERAIE-ATNAEITKlrSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1648 ISKLERNVEELKRKAAQNSGEAEYIEKVV---------YSVKQNADDVK------KTLDGELdEKYKKVESLiAQKTEES 1712
Cdd:pfam15921 571 IENMTQLVGQHGRTAGAMQVEKAQLEKEIndrrlelqeFKILKDKKDAKireleaRVSDLEL-EKVKLVNAG-SERLRAV 648
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1713 ADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQEL 1761
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-451 |
3.85e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 3.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 398 CTCDPAGSENGGiCDGYTdfsvgliaGQCRCKLHVEGERCDVCKEGFYDLSAED 451
Cdd:smart00180 1 CDCDPGGSASGT-CDPDT--------GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1202-1765 |
3.97e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1202 EKAKALKISGVIGPYRETVDSVEKKVNEIKDILAqspAAEPLKNIGILFEEAE-KLTKDVTEKMAQVEVKLT---DTASQ 1277
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQE---LKLLKDELELKKSEDLlKETQLVKLQEQLELLLSRqklEERSQ 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1278 SNSTAGELGA-----------LQAEAESLDKTVKELAEQLEFIKNSDIQGALDSITKyfQMSLEAEKRVNAST---TDPN 1343
Cdd:pfam02463 501 KESKARSGLKvllalikdgvgGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA--DEVEERQKLVRALTelpLGAR 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1344 STVEQSALTR-DRVEDLMLERESPFKEQQEEQA---RLLDELAGKLQSLDLSAVAQMtcGTPPGADCSESECGGPNCRTD 1419
Cdd:pfam02463 579 KLRLLIPKLKlPLKSIAVLEIDPILNLAQLDKAtleADEDDKRAKVVEGILKDTELT--KLKESAKAKESGLRKGVSLEE 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1420 EG-EKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNE 1498
Cdd:pfam02463 657 GLaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1499 DLRNLIKQIRNF-LTEDSADLDSIEAVANE---VLKMEMPS---TPQQLQNLTEDIRERveTLSQVEVILQQSAADIARA 1571
Cdd:pfam02463 737 ELKLLKQKIDEEeEEEEKSRLKKEEKEEEKselSLKEKELAeerEKTEKLKVEEEKEEK--LKAQEEELRALEEELKEEA 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1572 ELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIE-----------SETAASEET 1640
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLkeeeleeqklkDELESKEEK 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1641 LTNASQRISKLER---NVEELKRKAAQNSGEAEYIE------------------------KVVYSVKQNADDVKKTLDG- 1692
Cdd:pfam02463 895 EKEEKKELEEESQklnLLEEKENEIEERIKEEAEILlkyeeepeellleeadekekeennKEEEEERNKRLLLAKEELGk 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ----------ELDEKYKKVESLIAQKTEEsadarrKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELV 1762
Cdd:pfam02463 975 vnlmaieefeEKEERYNKDELEKERLEEE------KKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
...
gi 1666305206 1763 RLE 1765
Cdd:pfam02463 1049 RLE 1051
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1561-1780 |
4.54e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1561 LQQSAADIARAELL-LEEAKRASKsatdvkvtADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQnlltsIESETAAsEE 1639
Cdd:COG3064 5 LEEKAAEAAAQERLeQAEAEKRAA--------AEAEQKAKEEAEEERLAELEAKRQAEEEAREAK-----AEAEQRA-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1640 TLTNASQRISKLERNVEELKRKAAQnsgeaeyiekvvysvkQNADDVKKTLDGELDEKykkvESLIAQKtEESADARRKA 1719
Cdd:COG3064 71 LAAEAAKKLAEAEKAAAEAEKKAAA----------------EKAKAAKEAEAAAAAEK----AAAAAEK-EKAEEAKRKA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1720 EL---LQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:COG3064 130 EEeakRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAA 193
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1722-1785 |
5.59e-07 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 48.59 E-value: 5.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1722 LQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTC 1785
Cdd:cd22303 7 IKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTC 70
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
975-1026 |
5.87e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.73 E-value: 5.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 975 PCQCHHNIDTtdPEACDKETGRCLkCLYHTEGDHCQLCQYGYYGDALR-QDCR 1026
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1535-1707 |
6.15e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1535 STPQQLQNLTEdirervetLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTAdmvKEALEEAEKAQVAAEKAIK 1614
Cdd:COG1579 1 AMPEDLRALLD--------LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAA---KTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1615 QADEDIQGTQNLLTSIESE---TAASEEtLTNASQRISKLE-------RNVEELKRKAAQNSGEAEYIEKVVYSVKQNAD 1684
Cdd:COG1579 70 EVEARIKKYEEQLGNVRNNkeyEALQKE-IESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|...
gi 1666305206 1685 DVKKTLDGELDEKYKKVESLIAQ 1707
Cdd:COG1579 149 EELAELEAELEELEAEREELAAK 171
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1453-1733 |
6.30e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.83 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKmvsEAKVR----ADEAKQNAQDVLLKTNATKEKV----DKSNEDLRNLIKQIRNFLTEDSadlDSIEAV 1524
Cdd:NF041483 182 AARAEAERLAE---EARQRlgseAESARAEAEAILRRARKDAERLlnaaSTQAQEATDHAEQLRSSTAAES---DQARRQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1525 ANEVLKmempSTPQQLQNLTEDIRE-RVETLSQVEVILQQSAADIARAELLLEEAKRASKSATdvkvtADMVKEALEEAE 1603
Cdd:NF041483 256 AAELSR----AAEQRMQEAEEALREaRAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEI-----ARLVGEATKEAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1604 KAQVAAEKAIkqADEDIQGTQNLLTSIE-SETAASEETltnASQrISKLERNVEELKRKAAQN--------SGEAEYI-- 1672
Cdd:NF041483 327 ALKAEAEQAL--ADARAEAEKLVAEAAEkARTVAAEDT---AAQ-LAKAARTAEEVLTKASEDakattraaAEEAERIrr 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1673 --EKVVYSVKQNADDVKKTLDGELDEKYKKVEsliAQKTEESADARRkaelLQNEAKTLLAQA 1733
Cdd:NF041483 401 eaEAEADRLRGEAADQAEQLKGAAKDDTKEYR---AKTVELQEEARR----LRGEAEQLRAEA 456
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-973 |
6.32e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 47.73 E-value: 6.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 917 CPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNPSDFGGSC 973
Cdd:pfam00053 1 CDCNPHGSLSDT----C--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1449-1768 |
6.37e-07 |
|
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: 54.59 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RDVLSALAEVEQLSKMVSEAKVRADEAKqnaqdvllktnATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEV 1528
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLH-----------GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 LKMEMPSTP--QQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSA---------TDVKVTADMVKE 1597
Cdd:TIGR00618 235 LQQTQQSHAylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahikavTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1598 ALE--EAEKAQVAAEKAIKQADE-DIQGTQNLLTS-----IESETAASEETL--------TNASQRISKLERNVEELKRK 1661
Cdd:TIGR00618 315 ELQskMRSRAKLLMKRAAHVKQQsSIEEQRRLLQTlhsqeIHIRDAHEVATSireiscqqHTLTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1662 AAQNSGEAEYIEKVVYSV-----KQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSK 1736
Cdd:TIGR00618 395 LQSLCKELDILQREQATIdtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350
....*....|....*....|....*....|..
gi 1666305206 1737 LQLLEDLERKYEDNQKYLEDKAQELVRLEGEV 1768
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1443-1765 |
6.51e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 54.31 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1443 KAMDFDRDVLSALAEVEQLSKMVSEAKVRADE--AKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRnFLTEDSAdlds 1520
Cdd:pfam05622 88 KCEELEKEVLELQHRNEELTSLAEEAQALKDEmdILRESSDKVKKLEATVETYKKKLEDLGDLRRQVK-LLEERNA---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1521 ieavanevlkMEMPSTPQqlqnLTEDIRERVETLSQVEVILQQSAadiaraEL---LLEEAKRASKSATDVK-------- 1589
Cdd:pfam05622 163 ----------EYMQRTLQ----LEEELKKANALRGQLETYKRQVQ------ELhgkLSEESKKADKLEFEYKkleeklea 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1590 ---------VTADMVKEALEEAEKAQVaaekaikQADEDIQGTQNLLTSIESETAASEETLTNA-SQRISKLERNVEELK 1659
Cdd:pfam05622 223 lqkekerliIERDTLRETNEELRCAQL-------QQAELSQADALLSPSSDPGDNLAAEIMPAEiREKLIRLQHENKMLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1660 RKAaqnsgEAEYIEKVVySVKQNADDV---KKTLDGELDEKYKKVESLIAQ-------------KTEESADARRKAELLQ 1723
Cdd:pfam05622 296 LGQ-----EGSYRERLT-ELQQLLEDAnrrKNELETQNRLANQRILELQQQveelqkalqeqgsKAEDSSLLKQKLEEHL 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1724 NEAKTLLAQANSKLQLLEDLE--------RKYEDNQKYLEDKAQELVRLE 1765
Cdd:pfam05622 370 EKLHEAQSELQKKKEQIEELEpkqdsnlaQKIDELQEALRKKDEDMKAME 419
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1216-1759 |
7.84e-07 |
|
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: 54.46 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1216 YRETVDSVEKKVNEIKDILAQspaaeplknigilfeeaEKLTKDVTEKMAQVEVKLTDTASQSNSTAGeLGALQAEAESL 1295
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNG-----------------ELSAADAAVAKDRSELEALEDQHGAFLDAD-IETAAADQEQL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1296 DKTVKELAEQLEFIKNsdIQGALDSIT-KYFQMSLEAEKRVNASTTDPNSTVEQSALTRDR----VEDLMLERESPFKEQ 1370
Cdd:pfam12128 350 PSWQSELENLEERLKA--LTGKHQDVTaKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRqlavAEDDLQALESELREQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1371 QEEQARLLDE----LAGKLQSLDLS-AVAQMTCGTPPGADCSESECGgpNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAM 1445
Cdd:pfam12128 428 LEAGKLEFNEeeyrLKSRLGELKLRlNQATATPELLLQLENFDERIE--RAREEQEAANAEVERLQSELRQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1446 DFDRD-------VLSALAEVEQ---------LSKMVSEAKV-RADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQir 1508
Cdd:pfam12128 506 EALRQasrrleeRQSALDELELqlfpqagtlLHFLRKEAPDwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGV-- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1509 nfltedSADLDSIEAvanevlkmempstPQQLQnLTEDIRERvetLSQVEVILQQSAADIARAElllEEAKRASKsatdv 1588
Cdd:pfam12128 584 ------KLDLKRIDV-------------PEWAA-SEEELRER---LDKAEEALQSAREKQAAAE---EQLVQANG----- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1589 kvtadmvkeALEEAEKAQVAAEKAIKQADEDIQgtqNLLTSIESETAASEETLTN----ASQRISKLERNVEELKRKAAQ 1664
Cdd:pfam12128 633 ---------ELEKASREETFARTALKNARLDLR---RLFDEKQSEKDKKNKALAErkdsANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1665 NSgEAEYIEKVVYSVKQNAddVKKTLDGELDEKYKKVESLIAqKTEESADARRKAelLQNEAKTLLAQANSKLQLLEDLE 1744
Cdd:pfam12128 701 WL-EEQKEQKREARTEKQA--YWQVVEGALDAQLALLKAAIA-ARRSGAKAELKA--LETWYKRDLASLGVDPDVIAKLK 774
|
570
....*....|....*
gi 1666305206 1745 RKYEDNQKYLEDKAQ 1759
Cdd:pfam12128 775 REIRTLERKIERIAV 789
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1444-1761 |
7.90e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 53.88 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1444 AMDFDRDVLS-------ALAEVEQLSKMVSEA---KVRADEAKQNAQDV----------LLKTNATKEKVDK-SNEDLRN 1502
Cdd:pfam05701 214 ALAREQDKLNwekelkqAEEELQRLNQQLLSAkdlKSKLETASALLLDLkaelaaymesKLKEEADGEGNEKkTSTSIQA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1503 LIKQIRNFLTEDSAdldSIEAVANEV--LKMEMPSTPQQLQNLTED---IRERvETLSQVEVILQQSAADIARAELLLEE 1577
Cdd:pfam05701 294 ALASAKKELEEVKA---NIEKAKDEVncLRVAAASLRSELEKEKAElasLRQR-EGMASIAVSSLEAELNRTKSEIALVQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1578 AKRasKSATDVKV-TADMVKEALEEAEKAQVAAEKA---IKQADEDIQGTQNLLTSIESE-TAASEETL-TNASqriskl 1651
Cdd:pfam05701 370 AKE--KEAREKMVeLPKQLQQAAQEAEEAKSLAQAAreeLRKAKEEAEQAKAAASTVESRlEAVLKEIEaAKAS------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1652 ernvEELKRKAAQNSGEAEYIEKvvysvKQNADDVKK--TLD-GELDEKYKKvesliAQKTEESADARRKAELLQ-NEAK 1727
Cdd:pfam05701 442 ----EKLALAAIKALQESESSAE-----STNQEDSPRgvTLSlEEYYELSKR-----AHEAEELANKRVAEAVSQiEEAK 507
|
330 340 350
....*....|....*....|....*....|....
gi 1666305206 1728 tllaqaNSKLQLLEDLERKYEDnqkyLEDKAQEL 1761
Cdd:pfam05701 508 ------ESELRSLEKLEEVNRE----MEERKEAL 531
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1449-1752 |
7.99e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RDVLSALAE-VEQLSKMVSEAKVRADEAKQNAQDVLlktnatKEKVDKSNEDlRNLIKQIRNFLTEdsadLDSIEAVane 1527
Cdd:COG3096 863 RQQLDQLKEqLQLLNKLLPQANLLADETLADRLEEL------REELDAAQEA-QAFIQQHGKALAQ----LEPLVAV--- 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1528 vlkmeMPSTPQQLQNLTEDIRERVETLSQVEvilqqsaadiARAELLLEEAKRA-----SKSATDVKVTADMV---KEAL 1599
Cdd:COG3096 929 -----LQSDPEQFEQLQADYLQAKEQQRRLK----------QQIFALSEVVQRRphfsyEDAVGLLGENSDLNeklRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1600 EEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKL---------ER---NVEELKRKAAQNSG 1667
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadaeaeERariRRDELHEELSQNRS 1073
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1668 EAEYIEKVVYSVKQNADDVKKTLdGELDEKYKKVESLIAQKTEESADARRKA------------ELLQNEAKTL------ 1729
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSLQKRL-RKAERDYKQEREQVVQAKAGWCAVLRLArdndverrlhrrELAYLSADELrsmsdk 1152
|
330 340
....*....|....*....|....*....
gi 1666305206 1730 ------LAQANskLQLLEDLERKYEDNQK 1752
Cdd:COG3096 1153 algalrLAVAD--NEHLRDALRLSEDPRR 1179
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1459-1780 |
9.03e-07 |
|
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: 54.06 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKqNAQDVL----LKTNATKEKVDKSNEDLRNLIKQIRNF------LTEDSADLDSI-----EA 1523
Cdd:pfam10174 366 KQLQDLTEEKSTLAGEIR-DLKDMLdvkeRKINVLQKKIENLQEQLRDKDKQLAGLkervksLQTDSSNTDTAlttleEA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 VAN-----EVLKMEMPSTPQQLqnltediRERVETLSQVEVILQQSAaDIARAELLLEEAkraskSATDVKVTADMVKEA 1598
Cdd:pfam10174 445 LSEkeriiERLKEQREREDRER-------LEELESLKKENKDLKEKV-SALQPELTEKES-----SLIDLKEHASSLASS 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1599 LEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIEsETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEY---IEKV 1675
Cdd:pfam10174 512 GLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERllgILRE 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1676 VYSVKQNAD----DVKKTLDGELDEKYKKVESLIAQKTEESADA--------RRKAELLQNEAKTLLAQANSKL----QL 1739
Cdd:pfam10174 591 VENEKNDKDkkiaELESLTLRQMKEQNKKVANIKHGQQEMKKKGaqlleearRREDNLADNSQQLQLEELMGALektrQE 670
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1740 LEDLERKYEDNQKYLEDKAQELVRLEGEVR------------SLLKDISEKVA 1780
Cdd:pfam10174 671 LDATKARLSSTQQSLAEKDGHLTNLRAERRkqleeilemkqeALLAAISEKDA 723
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1547-1661 |
1.05e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 51.60 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1547 IRERVETLSQVEVILQQSaadIARAELLLEEAKRASKSA-TDVKVTADMVKEALEEAEKAQVAAEKAIKQADED------ 1619
Cdd:pfam04012 13 IHEGLDKAEDPEKMLEQA---IRDMQSELVKARQALAQTiARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEElareal 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1666305206 1620 --IQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRK 1661
Cdd:pfam04012 90 aeKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK 133
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1251-1774 |
1.10e-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: 53.82 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVTEKMAQVEVKLTDTaSQSNSTAGELGALQAEAEsldktvKELAEQLEFiknSDIQGALDSITKYFQMSLE 1330
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQA------TIDTRTSAF---RDLQGQLAHAKKQQELQQR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1331 AEKRVNASTTdpNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQS---LDLSAVAQMTCGTP--PGAD 1405
Cdd:TIGR00618 439 YAELCAAAIT--CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLarlLELQEEPCPLCGSCihPNPA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1406 CSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHsawqkamdfdrdvlsalaEVEQLSKMVSEAKVRADEAKQNAQDVLLK 1485
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH------------------QLTSERKQRASLKEQMQEIQQSFSILTQC 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1486 TNATKEKVDKsnedLRNLIKQIRNFLTEDSADLDSIeAVANEVLKMEMpSTPQQLQNLTEDIRERVETLSQVEVILQQSA 1565
Cdd:TIGR00618 579 DNRSKEDIPN----LQNITVRLQDLTEKLSEAEDML-ACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1566 ADIARAELllEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKaikqadEDIQGTQNLLTSIEsetaaseetltnas 1645
Cdd:TIGR00618 653 LTLTQERV--REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK------EMLAQCQTLLRELE-------------- 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1646 QRISKLERNVEElkrkaaqnsgeaeyIEKVVYSVKQnaddvkkTLDGELDEKYKKVESLIAQKtEESADARRKAELLQNE 1725
Cdd:TIGR00618 711 THIEEYDREFNE--------------IENASSSLGS-------DLAAREDALNQSLKELMHQA-RTVLKARTEAHFNNNE 768
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1726 AKTLLAQANSKLQlleDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKD 1774
Cdd:TIGR00618 769 EVTAALQTGAELS---HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1222-1777 |
1.48e-06 |
|
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: 53.51 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1222 SVEKKVNEIKDILAQSPAAEPLKNIGILF-------EEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAES 1294
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQgqkvqehQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1295 LDKTVKELAEQLEFIKNSDiqgalDSITKYFQMSLEAEKRvnasttdpNSTVEQSAL-----TRDRVEDLMLERESPFKE 1369
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLD-----NEIKALKSRKKQMEKD--------NSELELKMEkvfqgTDEQLNDLYHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1370 QQEEQARLLDELaGKL--QSLDLSAVAQMTcgtppgadcsESECGGPNCRTDEGEKKCGGPGCGGLVTVAHS---AWQKA 1444
Cdd:TIGR00606 317 KERELVDCQREL-EKLnkERRLLNQEKTEL----------LVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1445 MDFDRDVLSALA--------EVEQLSKMVSE-------AKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRN 1509
Cdd:TIGR00606 386 PFSERQIKNFHTlvierqedEAKTAAQLCADlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1510 fltedsadldsIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLL----EEAKRASKSA 1585
Cdd:TIGR00606 466 -----------LEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLdqemEQLNHHTTTR 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1586 TDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNL---LTSIESETAASEETLTNASQRISKLERNV----EEL 1658
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLedwLHSKSKEINQTRDRLAKLNKELASLEQNKnhinNEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1659 KRKAAQnsgEAEYIEKVVYSVKQNADDVK-KTLDGELDEKYKKV----------ESLIAQKTEESA--------DARRKA 1719
Cdd:TIGR00606 615 ESKEEQ---LSSYEDKLFDVCGSQDEESDlERLKEEIEKSSKQRamlagatavySQFITQLTDENQsccpvcqrVFQTEA 691
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 1720 EL------LQNEAKTLLAQANSKLQLLEDLERKYED-------NQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:TIGR00606 692 ELqefisdLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
510-548 |
1.56e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.58 E-value: 1.56e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1666305206 510 CDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYY 548
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1593-1777 |
1.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1593 DMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYI 1672
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1673 EkvVYSVKQNADDVKKTLDGELDEKYKKVESlIAQKTEESADARRKAELLQNEAKTLLAQ-ANSKLQLLEDLERKYEDNQ 1751
Cdd:COG4717 129 P--LYQELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*.
gi 1666305206 1752 KYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQ 231
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-387 |
2.34e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 2.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 335 CNCNEHSS---SCHFDmavflatgnvsGGVCDnCQHNTMGRNCEQCKPFYFQHPER 387
Cdd:cd00055 2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1492-1745 |
2.84e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1492 KVDKSNEDLRNLIKQirnFLTEDSADL-DSIEAVANEVLK-----MempsTPQQLQNLTEDIRERVETLSQVEV------ 1559
Cdd:COG2268 98 KVNSDPEDIANAAER---FLGRDPEEIeELAEEKLEGALRavaaqM----TVEELNEDREKFAEKVQEVAGTDLakngle 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1560 --------ILQQS----------------AADIARAELLLEEA---KRASKSATDVKVTADMvkeALEEAEKAQVAAEKA 1612
Cdd:COG2268 171 lesvaitdLEDENnyldalgrrkiaeiirDARIAEAEAERETEiaiAQANREAEEAELEQER---EIETARIAEAEAELA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1613 IKQADEDIQGTQnllTSIESETAASEETlTNASQRIsklERNVEELKRKAAQNSGEAEyIEKvvySVKQNADDVKKTLDG 1692
Cdd:COG2268 248 KKKAEERREAET---ARAEAEAAYEIAE-ANAEREV---QRQLEIAEREREIELQEKE-AER---EEAELEADVRKPAEA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1693 EldeKYKKVESLIAQKTEESADARRKAELLQ--NEAKTLLAQANSKLQLLEDLER 1745
Cdd:COG2268 317 E---KQAAEAEAEAEAEAIRAKGLAEAEGKRalAEAWNKLGDAAILLMLIEKLPE 368
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1592-1771 |
2.96e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.21 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 ADMVK----EALEEAEKAQVAAEKAIKQADEDIQgtqnlltSIESETA---ASEETLTnasQRISKLERNVEELKRKA-- 1662
Cdd:COG1842 7 SDIIRaninALLDKAEDPEKMLDQAIRDMEEDLV-------EARQALAqviANQKRLE---RQLEELEAEAEKWEEKArl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1663 AQNSGE----AEYIEKVVySVKQNADDVKKTLDgELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTllAQANSKLQ 1738
Cdd:COG1842 77 ALEKGRedlaREALERKA-ELEAQAEALEAQLA-QLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKA--AKAQEKVN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1739 ----------LLEDLERkYEDNQKYLEDKAQ---ELVR---LEGEVRSL 1771
Cdd:COG1842 153 ealsgidsddATSALER-MEEKIEEMEARAEaaaELAAgdsLDDELAEL 200
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
335-385 |
2.98e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 2.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 335 CNCNEHSS---SCHFdmavflatgnvSGGVCDnCQHNTMGRNCEQCKPFYFQHP 385
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1545-1781 |
3.11e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.96 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1545 EDIRERVETLSQVEVILQQS---AADIARAE--LLLEEAKRASKSATDVKV-TADMVKEALEEAEKAQVAAEKAIKQADE 1618
Cdd:COG3064 12 AAAQERLEQAEAEKRAAAEAeqkAKEEAEEErlAELEAKRQAEEEAREAKAeAEQRAAELAAEAAKKLAEAEKAAAEAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1619 DIQGTQNLLTSiESETAASEETLTNASQ--RISKLERNVEE-LKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELD 1695
Cdd:COG3064 92 KAAAEKAKAAK-EAEAAAAAEKAAAAAEkeKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1696 EKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDI 1775
Cdd:COG3064 171 AARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250
|
....*.
gi 1666305206 1776 SEKVAV 1781
Cdd:COG3064 251 AADLAA 256
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1442-1786 |
3.26e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.53 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1442 QKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLlktNATKEKVDKSNEDLRNLIKQIRNfltedsadLDSI 1521
Cdd:PTZ00440 1084 EKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHY---NKKKKSLEKIYKQMEKTLKELEN--------MNLE 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1522 EAVANEVLKMEMPSTPQQLQNLTEDIRERVEtlsqvevilqqsaadiaRAELLLEEAKRASKSATDVKVtaDMVKEALEE 1601
Cdd:PTZ00440 1153 DITLNEVNEIEIEYERILIDHIVEQINNEAK-----------------KSKTIMEEIESYKKDIDQVKK--NMSKERNDH 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 AE--KAQVAAEKAIkQADEDIQgtqNLLTSiesetAASEETLTNASQRISKLERNVEELKrkaaqnsgeaEYIEKvvysV 1679
Cdd:PTZ00440 1214 LTtfEYNAYYDKAT-ASYENIE---ELTTE-----AKGLKGEANRSTNVDELKEIKLQVF----------SYLQQ----V 1270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1680 KQNADDVKKTLdGELDEKYKKVESLIAQK-TEESADARRKAELLQNEAKTLLAQANsklQLLEDLERKYEDNQKY----- 1753
Cdd:PTZ00440 1271 IKENNKMENAL-HEIKNMYEFLISIDSEKiLKEILNSTKKAEEFSNDAKKELEKTD---NLIKQVEAKIEQAKEHknkiy 1346
|
330 340 350
....*....|....*....|....*....|....*...
gi 1666305206 1754 --LEDKaqelvRLEGEVRSLL---KDISEKVAVYSTCL 1786
Cdd:PTZ00440 1347 gsLEDK-----QIDDEIKKIEqikEEISNKRKEINKYL 1379
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1456-1691 |
3.43e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 51.94 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVlkmemps 1535
Cdd:COG0840 288 ASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESS------- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1536 tpQQLQNLTEDIRErvetlsqvevILQQS------AAdI--ARA---------------ELlleeAKRASKSATDVKvta 1592
Cdd:COG0840 361 --QEIGEIVDVIDD----------IAEQTnllalnAA-IeaARAgeagrgfavvadevrKL----AERSAEATKEIE--- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1593 DMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEET------LTNASQRISK----LERNVEELKRKA 1662
Cdd:COG0840 421 ELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVsdliqeIAAASEEQSAgteeVNQAIEQIAAAA 500
|
250 260
....*....|....*....|....*....
gi 1666305206 1663 AQNSGEAEYIEKVVYSVKQNADDVKKTLD 1691
Cdd:COG0840 501 QENAASVEEVAAAAEELAELAEELQELVS 529
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1628-1778 |
3.88e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1628 TSIESETAASEETLTNASQRISKLERNVEELKRKAAQNS-----------------GEAEYIEKVVYSVKQNADDVKKTL 1690
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCeeknalqeqlqaetelcAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1691 DGELDEKYKKVESLIAQKT-------------EESADARRKAEL--LQNEAKT--------LLAQANSKLQ----LLEDL 1743
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKkmqqhiqdleeqlDEEEAARQKLQLekVTTEAKIkkleedilLLEDQNSKLSkerkLLEER 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1666305206 1744 ERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEER 195
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1221-1779 |
3.95e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1221 DSVEKKVNEIKDILAQ-SPAAEPLKNigiLFEEAEKLTKDVTEKMAQVE---VKLTDTASQSNSTAGELGALQAEAESld 1296
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEiSNTQTQLNQ---LKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLNNQKEQ-- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1297 KTVKELAEQLEFIKN--SDIQGALD----SITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKE- 1369
Cdd:TIGR04523 307 DWNKELKSELKNQEKklEEIQNQISqnnkIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEi 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1370 ---------------QQEEQARLLDElagKLQSLdlsavaqmtcgtppgadcsESEcggpncrtdegekkcggpgcgglv 1434
Cdd:TIGR04523 387 knlesqindleskiqNQEKLNQQKDE---QIKKL-------------------QQE------------------------ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1435 tvaHSAWQKamdfdrdvlsalaEVEQLSKMVSEAKvraDEAKQ-NAQDVLLKT-----NATKEKVDKSNEDLRNLIKQIR 1508
Cdd:TIGR04523 421 ---KELLEK-------------EIERLKETIIKNN---SEIKDlTNQDSVKELiiknlDNTRESLETQLKVLSRSINKIK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1509 NFLTEDSADLDS----IEAVANEVLKMEmpstpQQLQNLTEDIRERVETLSQVEvilqqsaADIARAELLLEEAKRASKS 1584
Cdd:TIGR04523 482 QNLEQKQKELKSkekeLKKLNEEKKELE-----EKVKDLTKKISSLKEKIEKLE-------SEKKEKESKISDLEDELNK 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1585 ATDVKVTADMVKE------ALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETltnasqrISKLERNVEEL 1658
Cdd:TIGR04523 550 DDFELKKENLEKEideknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK-------ISSLEKELEKA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1659 KRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDG------ELDEKYKKVESLIAQKTEESADArrKAELLQNEAKTLLAQ 1732
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEirnkwpEIIKKIKESKTKIDDIIELMKDW--LKELSLHYKKYITRM 700
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1666305206 1733 A-NSKLQLLEDLERKYEDNQKYLEDKAQELVrlegevrSLLKDISEKV 1779
Cdd:TIGR04523 701 IrIKDLPKLEEKYKEIEKELKKLDEFSKELE-------NIIKNFNKKF 741
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1617-1782 |
4.32e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1617 DEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEyiekvvySVKQNADDVKKTLDG---- 1692
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 -ELDEKYKKVESLIAQKTEESADARRKAELLQnEAKTLLAQANSKLQLLE-DLERKYEDNQKYLEDKAQELVRLEGEVRS 1770
Cdd:COG1579 89 kEYEALQKEIESLKRRISDLEDEILELMERIE-ELEEELAELEAELAELEaELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|...
gi 1666305206 1771 LLKDISEK-VAVY 1782
Cdd:COG1579 168 LAAKIPPElLALY 180
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1447-1749 |
4.61e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.55 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1447 FDRDVLSALAEVEQLSKMVSEAKVRA-DEAKQNAQDVLLKTNATKE--------KVDKSN-EDLRNLIKQIRNFLTEDSA 1516
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEEAEKKAkDQKEEDRRNYPTNTYKTLEleiaesdvEVKKAElELVKEEAKEPRDEEKIKQA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1517 DlDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAEL---LLEEAKRASKSATDVKVTAD 1593
Cdd:NF033838 210 K-AKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAkrgVLGEPATPDKKENDAKSSDS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1594 MVKE------------ALEEAEKAQVAAEKAIK-QADEDIQG-TQNLLTSIESETAASEETLTNASQRISKLE----RNV 1655
Cdd:NF033838 289 SVGEetlpspslkpekKVAEAEKKVEEAKKKAKdQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEEakepRNE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 EELKRKAAQ---NSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAEllqNEAKTLLAQ 1732
Cdd:NF033838 369 EKIKQAKAKvesKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPE---KPAEQPKAE 445
|
330
....*....|....*..
gi 1666305206 1733 ANSKLQLLEDLERKYED 1749
Cdd:NF033838 446 KPADQQAEEDYARRSEE 462
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1450-1671 |
5.67e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1450 DVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRnfltEDSADLDSIEAVANevl 1529
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY----RSGGSVSYLDVLLG--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1530 kmempSTpqqlqNLTEDIrERVETLSQV----EVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKA 1605
Cdd:COG3883 111 -----SE-----SFSDFL-DRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 1606 QvaaEKAIKQADEDIQGTQNLLTSIESETAASEETLTnASQRISKLERNVEELKRKAAQNSGEAEY 1671
Cdd:COG3883 180 Q---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA-AAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| Mt_ATP_synt |
pfam15704 |
Mitochondrial ATP synthase subunit; This plant mitochondrial ATP synthase subunit may the the ... |
1472-1665 |
7.04e-06 |
|
Mitochondrial ATP synthase subunit; This plant mitochondrial ATP synthase subunit may the the equivalent of the mitochondrial ATP synthase d subunit.
Pssm-ID: 406195 [Multi-domain] Cd Length: 188 Bit Score: 48.61 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1472 ADEAKQNAQDVLLKtnatkEKVDKSNEDLRNLIKQIRNF-LTEDSADLDSIEAVANEVL----KMEMPSTPQQLQNLted 1546
Cdd:pfam15704 4 AAEPKALAGDDVVK-----SVFIEVQKKFRALLGVLRKEkITIDPGDPAAVKAYAAVMKaarkKAGLPSPSQRIKET--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1547 irervetlsqveviLQQSAADIARAELLLEEAK--RASKSATDVKVTADMVKEALEEAEKaqvAAEKAIKQADEdiQGTQ 1624
Cdd:pfam15704 76 --------------IEGATQEIPDVRTFLEKLGeiRIKRGLEDELGAEALMMEALDKVEK---AIGKPLLRSDK--KGMA 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1666305206 1625 NLltsiESETAASEETLTNASQRISKLErnvEELKRKAAQN 1665
Cdd:pfam15704 137 LL----TAEFDKINKKLGIRKEDLPKYE---EELELEIAKA 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1449-1698 |
7.11e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RDVLSALAEVEQLSKM--VSEAKVRadEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVAN 1526
Cdd:PHA02562 153 RKLVEDLLDISVLSEMdkLNKDKIR--ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1527 EvLKMEMPSTPQQLQNLTEDIRERVETLSQveviLQQSAADI-ARAELLLEEAKRASK-----------SATDVKVT--A 1592
Cdd:PHA02562 231 T-IKAEIEELTDELLNLVMDIEDPSAALNK----LNTAAAKIkSKIEQFQKVIKMYEKggvcptctqqiSEGPDRITkiK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1593 DMVKEALEEAEKAQVAAEKAIKQADEdIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKrkaAQNSGEAEYI 1672
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDE-FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ---AEFVDNAEEL 381
|
250 260
....*....|....*....|....*.
gi 1666305206 1673 EKVVysvkQNADDVKKTLDGELDEKY 1698
Cdd:PHA02562 382 AKLQ----DELDKIVKTKSELVKEKY 403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1548-1764 |
7.28e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1548 RERVETLsqvEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEaekaqvaaEKAIKQADEDIQGTQNLL 1627
Cdd:COG4913 609 RAKLAAL---EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD--------EIDVASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1628 TSIEsetaASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGeldekykkVESLIAQ 1707
Cdd:COG4913 678 ERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA--------AEDLARL 745
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1708 KTEESADARRKAELLQNEAKtllaqansklQLLEDLERKYEDNQKYLEDKAQELVRL 1764
Cdd:COG4913 746 ELRALLEERFAAALGDAVER----------ELRENLEERIDALRARLNRAEEELERA 792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1490-1769 |
8.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KEKVDKSNEDLRNLIKQIRNfLTEDSADLDSIEAVAnEVLKME--MPSTPQQLQNLTEDIRERVETLSQVEVILQQSAAD 1567
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIID-EDIDGNHEGKAEAKA-HVGQDEglKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1568 IARAElllEE--AKRASKSATDVKvTADMVKEA-----LEEAEKAQVAAEKAIKQADEDIQgtqnlltSIESETAASEET 1640
Cdd:PTZ00121 1108 TGKAE---EArkAEEAKKKAEDAR-KAEEARKAedarkAEEARKAEDAKRVEIARKAEDAR-------KAEEARKAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1641 LTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVvysvkQNADDVKKTLDGELDEKYKKVESliAQKTEEsaDARRKAE 1720
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE-----RKAEEARKAEDAKKAEAVKKAEE--AKKDAE--EAKKAEE 1247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1721 LLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVR 1769
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1451-1773 |
8.21e-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: 50.73 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1451 VLSALAEVEQLSKMV-SEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLI-KQIRNFLTEDSADLDSIEAVANEV 1528
Cdd:COG5185 133 LKDELIKVEKLDEIAdIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGlLKGISELKKAEPSGTVNSIKESET 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 LKMEMPSTPqqLQNLTEDIrERVETLSQVEVIlQQSAADIARAELLLEEA--KRASKSATDVKVTADMVKEALEEAEKAQ 1606
Cdd:COG5185 213 GNLGSESTL--LEKAKEII-NIEEALKGFQDP-ESELEDLAQTSDKLEKLveQNTDLRLEKLGENAESSKRLNENANNLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1607 VAAEKAIKQADEDIQgTQNLLTSIES--ETAASEETLTNASQRISKLERNVEELKRKAAQ-NSGEAEYIEKVVYSVKQ-- 1681
Cdd:COG5185 289 KQFENTKEKIAEYTK-SIDIKKATESleEQLAAAEAEQELEESKRETETGIQNLTAEIEQgQESLTENLEAIKEEIENiv 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1682 ---NADDVKKTLDGELDEKYKKVESLIAQKTeesaDARRKA-ELLQNEAKTLLAQANSKLQL---LEDLERKYEDNQKYL 1754
Cdd:COG5185 368 gevELSKSSEELDSFKDTIESTKESLDEIPQ----NQRGYAqEILATLEDTLKAADRQIEELqrqIEQATSSNEEVSKLL 443
|
330
....*....|....*....
gi 1666305206 1755 EDKAQELVRLEGEVRSLLK 1773
Cdd:COG5185 444 NELISELNKVMREADEESQ 462
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1484-1770 |
1.11e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1484 LKTNATKEKVDKSneDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKME--MPSTpqqLQNLTEDIRERVETLSQVEVIL 1561
Cdd:PTZ00440 328 IQNNNIPPQVKKD--ELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEkiLNNL---FNKLFGDLKEKIETLLDSEYFI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1562 QQSAADIARAELLLEEAKRASKSAT---------------DVKVTADMVKEALEEA--------------------EKAQ 1606
Cdd:PTZ00440 403 SKYTNIISLSEHTLKAAEDVLKENSqkiadyalysnleiiEIKKKYDEKINELKKSinqlktlisimksfydliisEKDS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1607 VAAEKAIKQADED-IQGTQNLL---TSIESETAASEETLTNAS-----------------QRISKLERNVEELKRKAAQN 1665
Cdd:PTZ00440 483 MDSKEKKESSDSNyQEKVDELLqiiNSIKEKNNIVNNNFKNIEdyyitieglkneiegliELIKYYLQSIETLIKDEKLK 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1666 SGEAEYIEKVVYSVKQNADDVKK--TLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQ--ANSKLQLLE 1741
Cdd:PTZ00440 563 RSMKNDIKNKIKYIEENVDHIKDiiSLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKfyKGDLQELLD 642
|
330 340 350
....*....|....*....|....*....|.
gi 1666305206 1742 DLERKYEDNQKYLEDK--AQELVRLEGEVRS 1770
Cdd:PTZ00440 643 ELSHFLDDHKYLYHEAksKEDLQTLLNTSKN 673
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
271-323 |
1.13e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.27 E-value: 1.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 271 CFCYGHAS---ECAPVDGvneevegmvhgHCMCRHNTKGLNCELCMDFYHDLPWRP 323
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTG-----------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1456-1658 |
1.30e-05 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 48.00 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSN---EDLRNLIKQIRNFLT--EDSAD------LD-SIEA 1523
Cdd:cd11386 12 ASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVsavEELEESSAEIGEIVEviDDIAEqtnllaLNaAIEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 ------------VANEVLKMempstPQQLQNLTEDIRERVETLsqvevilqqsAADIARAellLEEAKRASKSATDVKVT 1591
Cdd:cd11386 92 arageagrgfavVADEVRKL-----AEESAEAAKEIEELIEEI----------QEQTEEA---VEAMEETSEEVEEGVEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 1592 ADMVKEALEEaekaqvaaekaIKQADEDIQgtqnllTSIESETAASEEtLTNASQRISkleRNVEEL 1658
Cdd:cd11386 154 VEETGRAFEE-----------IVASVEEVA------DGIQEISAATQE-QSASTQEIA---AAVEEI 199
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1456-1774 |
1.49e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDV--------LLKTNATKEKVDKSNEDLRNLiKQIRNFLTEDSADLDSIEAVANe 1527
Cdd:PRK04863 851 RALADHESQEQQQRSQLEQAKEGLSALnrllprlnLLADETLADRVEEIREQLDEA-EEAKRFVQQHGNALAQLEPIVS- 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1528 VLKmempSTPQQLQNLTEDIRERVETLSQVevilQQSAADIA-----RAELLLEEA-KRASKSATDVkvtaDMVKEALEE 1601
Cdd:PRK04863 929 VLQ----SDPEQFEQLKQDYQQAQQTQRDA----KQQAFALTevvqrRAHFSYEDAaEMLAKNSDLN----EKLRQRLEQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 AEKAQVAAEKAIKQADEdiQGTQN--LLTSIESETAASEETLTNASQRISKLE-RNVEELKRKAA-----------QNSG 1667
Cdd:PRK04863 997 AEQERTRAREQLRQAQA--QLAQYnqVLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEERARarrdelharlsANRS 1074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1668 EAEYIEKVVYSVKQNADDVKKTLDgELDEKYKKV-ESLIAQK--------------TEESADARRKAELLQNEAKTLLAQ 1732
Cdd:PRK04863 1075 RRNQLEKQLTFCEAEMDNLTKKLR-KLERDYHEMrEQVVNAKagwcavlrlvkdngVERRLHRRELAYLSADELRSMSDK 1153
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1733 ANSKLQL-------LEDLERKYEDNqKYLEDKAQELVRlegeVRSLLKD 1774
Cdd:PRK04863 1154 ALGALRLavadnehLRDVLRLSEDP-KRPERKVQFYIA----VYQHLRE 1197
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1453-1664 |
1.53e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 49.63 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNF------LTEDSADLD------- 1519
Cdd:COG0840 292 ETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETaetieeLGESSQEIGeivdvid 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1520 -------------SIEA------------VANEVLKMEmpstpQQLQNLTEDIRERVETLsqvevilQQSAADIARA-EL 1573
Cdd:COG0840 372 diaeqtnllalnaAIEAarageagrgfavVADEVRKLA-----ERSAEATKEIEELIEEI-------QSETEEAVEAmEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1574 LLEEAKRASKSATDVKVTADMVKEALEE-AEKAQVAAEKAIKQAdediQGTQNLLTSIESETAASEET---LTNASQRIS 1649
Cdd:COG0840 440 GSEEVEEGVELVEEAGEALEEIVEAVEEvSDLIQEIAAASEEQS----AGTEEVNQAIEQIAAAAQENaasVEEVAAAAE 515
|
250
....*....|....*
gi 1666305206 1650 KLERNVEELKRKAAQ 1664
Cdd:COG0840 516 ELAELAEELQELVSR 530
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1519-1657 |
1.64e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 49.63 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1519 DSIEAVANEVLKMEmpstpQQLQNLTEDIRERVETLSQVEVILQQSAADIA-RAELLLEEAKRASKSATDVKVT----AD 1593
Cdd:COG0840 235 DEIGQLADAFNRMI-----ENLRELVGQVRESAEQVASASEELAASAEELAaGAEEQAASLEETAAAMEELSATvqevAE 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1594 MVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESetaaseetltnASQRISKLERNVEE 1657
Cdd:COG0840 310 NAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE-----------TAETIEELGESSQE 362
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1592-1780 |
1.84e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 47.75 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 ADMVKEALEEAEKAQVAAEKAIKQADEDIQgtqnlltsieSETAASEETLTNASQRISKLERNVEELKR---------KA 1662
Cdd:pfam04012 6 GRLVRANIHEGLDKAEDPEKMLEQAIRDMQ----------SELVKARQALAQTIARQKQLERRLEQQTEqakkleekaQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1663 AQNSGEAEYIEKVVYSVKQNADDVKktldgELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKlqlled 1742
Cdd:pfam04012 76 ALTKGNEELAREALAEKKSLEKQAE-----ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA------ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1666305206 1743 lerkyednqkyledKAQELV-------RLEGEVRSlLKDISEKVA 1780
Cdd:pfam04012 145 --------------KAQEAVqtslgslSTSSATDS-FERIEEKIE 174
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1445-1778 |
2.18e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.83 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1445 MDFDRDVLSALAEVEQLSKMVSEAKVRaDEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRnfLTEDSADLDSIEA- 1523
Cdd:PTZ00440 1454 IKYEKEITNILNNSSILGKKTKLEKKK-KEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPN--IKREGDVLNNDKSt 1530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 VANEVLKMEMPSTPQQLQNLTeDIRERVETLSQVEVILQQSAADIAR--AELLLEEAKraSKSATDVKVTADMVKEalee 1601
Cdd:PTZ00440 1531 IAYETIQYNLGRVKHNLLNIL-NIKDEIETILNKAQDLMRDISKISKivENKNLENLN--DKEADYVKYLDNILKE---- 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1602 aEKAQVAAEKAIKQADEDIQGTQNLLTS--IESETAASEETLTNASQRISKLERNVEELKRKAAQNSG--EAEYIEKvvY 1677
Cdd:PTZ00440 1604 -KQLMEAEYKKLNEIYSDVDNIEKELKKhkKNYEIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSSlfNNFYLNK--Y 1680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1678 SVKQNADDVKKTLD---GELDEKYKKVESLIAQKTEESADArrkaellqNEAKTLlaqaNSKLQLLED-LERKYEDNQKY 1753
Cdd:PTZ00440 1681 NINENLEKYKKKLNeiyNEFMESYNIIQEKMKEVSNDDVDY--------NEAKTL----REEAQKEEVnLNNKEEEAKKY 1748
|
330 340
....*....|....*....|....*.
gi 1666305206 1754 LED-KAQELVRLEGEVRSLLKDISEK 1778
Cdd:PTZ00440 1749 LNDiKKQESFRFILYMKEKLDELSKM 1774
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
867-906 |
2.47e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1666305206 867 CQCN--GHALD-CDTVTGECLsCQDYTTGHNCERCLAGYYGDP 906
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1479-1784 |
2.54e-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: 49.27 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1479 AQDVLLKTNATKEKVDKSNEDlRNLIKQIRNFLT------EDSA--------DLDSIEAVANEV---LKMEMPSTPQQLQ 1541
Cdd:TIGR00606 365 ARDSLIQSLATRLELDGFERG-PFSERQIKNFHTlvierqEDEAktaaqlcaDLQSKERLKQEQadeIRDEKKGLGRTIE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1542 NLTEDIRERVETLSQVEVILQQSAADIARaelLLEEAKRASKSATDVKVTAdmvKEALEEAEKAQVaaekaikqadediq 1621
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQLEGSSDR---ILELDQELRKAERELSKAE---KNSLTETLKKEV-------------- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1622 gtqnllTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKvVYSVKQNADDVKKTLDGELDEKyKKV 1701
Cdd:TIGR00606 504 ------KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLGYFPNK-KQL 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1702 ESLIAQKTEESADARRKAELLQNE---AKTLLAQANSKLQLLEDLERKYEDNQKYL---EDKAQELVRLEGEVRSLLKD- 1774
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKElasLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQr 655
|
330
....*....|..
gi 1666305206 1775 --ISEKVAVYST 1784
Cdd:TIGR00606 656 amLAGATAVYSQ 667
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1548-1768 |
2.66e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1548 RERVETLSQVEVILQQSAADIARAE--LLLEEAKRASKSATDVKVTadmvkEALEEAEKAQVAAEKAI-----KQADEDI 1620
Cdd:COG3064 59 EAKAEAEQRAAELAAEAAKKLAEAEkaAAEAEKKAAAEKAKAAKEA-----EAAAAAEKAAAAAEKEKaeeakRKAEEEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1621 QGTQNlLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKK 1700
Cdd:COG3064 134 KRKAE-EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1701 VESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEV 1768
Cdd:COG3064 213 DAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1569-1765 |
2.87e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1569 ARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRI 1648
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1649 SKLERNVEELKRKAAQNSGEAEYIEKVVysvkqnadDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKT 1728
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEK--------KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1666305206 1729 LLAQANSK-------LQLLEDLERKYEDNQKYLEDKAQELVRLE 1765
Cdd:pfam02463 326 AEKELKKEkeeieelEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-974 |
3.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 42.73 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 916 PCPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNPSDfGGSCQ 974
Cdd:cd00055 1 PCDCNGHGSLSGQ----C--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1562-1737 |
4.05e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 48.33 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1562 QQSAADI-----ARAELLLEEAKRASKSatdvkVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLT-------- 1628
Cdd:PRK00106 41 EQEAVNLrgkaeRDAEHIKKTAKRESKA-----LKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTeratsldr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1629 ------SIESETAASEETLTNASQRISKLERNVEELKRKaaqnsgEAEYIEKVVYSVKQNADDVKktldgeLDEKYKKVE 1702
Cdd:PRK00106 116 kdenlsSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQ------KKAELERVAALSQAEAREII------LAETENKLT 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1666305206 1703 SLIAQKTEESadARRKAELLQNEAKTLLAQANSKL 1737
Cdd:PRK00106 184 HEIATRIREA--EREVKDRSDKMAKDLLAQAMQRL 216
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1474-1630 |
4.26e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 48.33 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1474 EAKQNAQDVLL--KTNATK--EKVDKSNEDLRNLIKQIRNFLTEDSADLD-SIEAVANEVLKMEmpSTPQQLQNLTEDIR 1548
Cdd:PRK00106 65 ESKALKKELLLeaKEEARKyrEEIEQEFKSERQELKQIESRLTERATSLDrKDENLSSKEKTLE--SKEQSLTDKSKHID 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1549 ERVETLSQVEvilQQSAADIAR-AELLLEEAKRASKSATDVKVTADM---VKEALEEA-EKAQVAAEKAIKQADEDIQG- 1622
Cdd:PRK00106 143 EREEQVEKLE---EQKKAELERvAALSQAEAREIILAETENKLTHEIatrIREAEREVkDRSDKMAKDLLAQAMQRLAGe 219
|
170
....*....|
gi 1666305206 1623 --TQNLLTSI 1630
Cdd:PRK00106 220 yvTEQTITTV 229
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1491-1779 |
4.39e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 47.02 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1491 EKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEavaneVLKmempstpQQLQNLTEDIRERVETLSQVevilqqsaadIAR 1570
Cdd:pfam06008 12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIE-----ILE-------KELSSLAQETEELQKKATQT----------LAK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1571 AELLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQAdediqgtqnlLTSIESETAASEETLTNASQRISK 1650
Cdd:pfam06008 70 AQQVNAESERTLGHA----------KELAEAIKNLIDNIKEINEKV----------ATLGENDFALPSSDLSRMLAEAQR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1651 LernVEELKrkaAQNSGEAeyiekvvysvKQNADDVKKtldgELDEKYKKVESLIAQKTEESadarrkaELLQNEAKTLL 1730
Cdd:pfam06008 130 M---LGEIR---SRDFGTQ----------LQNAEAELK----AAQDLLSRIQTWFQSPQEEN-------KALANALRDSL 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1731 AQANSKLQLLEDLERKyednqkyLEDKAQELVRLEGEVRSLLKDISEKV 1779
Cdd:pfam06008 183 AEYEAKLSDLRELLRE-------AAAKTRDANRLNLANQANLREFQRKK 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1483-1777 |
4.63e-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: 48.48 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1483 LLKTNATKEKvdksneDLRNLIKQIRNFLTEDSADLDSIEAVANEvlKMEmpstpqQLQNLTEDIRervetlsqvevILQ 1562
Cdd:TIGR04523 27 IANKQDTEEK------QLEKKLKTIKNELKNKEKELKNLDKNLNK--DEE------KINNSNNKIK-----------ILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1563 QSAADIARAelLLEEAKRASKsatdvkVTADMVKEALEEAEKAQ--VAAEKAIKQADEDIQGTQNLLTSIESETAASEET 1640
Cdd:TIGR04523 82 QQIKDLNDK--LKKNKDKINK------LNSDLSKINSEIKNDKEqkNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1641 LTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQ--NADDVKKTLDGELDEKYKKVESLIAQKTEESADARRK 1718
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNklLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1719 AELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1207-1761 |
4.85e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1207 LKISGVIGPYRETVDSVEKKVNEIKDILAqspaaePLKNigilFEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELG 1286
Cdd:PTZ00440 439 LEIIEIKKKYDEKINELKKSINQLKTLIS------IMKS----FYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIIN 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1287 ALQAEAESLD---KTVKELAEQLEFIKNsDIQGALDSITKYFQ--MSL-EAEKRVNASTTDPNSTVEQSALTRDRVEDLM 1360
Cdd:PTZ00440 509 SIKEKNNIVNnnfKNIEDYYITIEGLKN-EIEGLIELIKYYLQsiETLiKDEKLKRSMKNDIKNKIKYIEENVDHIKDII 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1361 LERESPFKEQQEEQarlldelagKLQSLDLSAVAQMTcgtppgadcsesecggpncrtdeGEKKCGGPGCGGLVTVAHSA 1440
Cdd:PTZ00440 588 SLNDEIDNIIQQIE---------ELINEALFNKEKFI-----------------------NEKNDLQEKVKYILNKFYKG 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1441 wqkamDFDRDVLSALAEVEQLSKMVSEAKvradeAKQNAQDVLLKTNATKEKVDKSNEDLrnlIKQIRNFLTEDSADL-- 1518
Cdd:PTZ00440 636 -----DLQELLDELSHFLDDHKYLYHEAK-----SKEDLQTLLNTSKNEYEKLEFMKSDN---IDNIIKNLKKELQNLls 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1519 --DSIEAVANEVLKMEMPSTPQQLQNLTEDIRERvetlsqvevilqqsaadiaraellLEEAKRASKSATDVKVTADMVK 1596
Cdd:PTZ00440 703 lkENIIKKQLNNIEQDISNSLNQYTIKYNDLKSS------------------------IEEYKEEEEKLEVYKHQIINRK 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1597 EA----LEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEaeyI 1672
Cdd:PTZ00440 759 NEfilhLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEE---L 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1673 EKVVYSVKQNADDVK-KTLDGELDEKYKKVESLIAQKTEESadarRKAELLQNEAKTLLAqANSKLQLLEDLERKYEDNQ 1751
Cdd:PTZ00440 836 KQLLQKFPTEDENLNlKELEKEFNENNQIVDNIIKDIENMN----KNINIIKTLNIAINR-SNSNKQLVEHLLNNKIDLK 910
|
570
....*....|
gi 1666305206 1752 KYLEDKAQEL 1761
Cdd:PTZ00440 911 NKLEQHMKII 920
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-388 |
5.01e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 5.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1666305206 335 CNCNE---HSSSCHFDmavflatgnvsGGVCDnCQHNTMGRNCEQCKPFYFQHPERD 388
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1456-1774 |
5.59e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAKVRADEAKQNAQDVL---LKTNATK-----EKVDKSNEDLRNLIKQIRnfltedsadldsieavANE 1527
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELeeqIEEREQKrqeeyEEKLQEREQMDEIVERIQ----------------EED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1528 VLKMEmpstpqqlqnltEDIRERVETLSQVEVILQQSAA--DIARAELLLEEAKRAsksATDVKVTAdmvKEALEEAEKA 1605
Cdd:pfam13868 115 QAEAE------------EKLEKQRQLREEIDEFNEEQAEwkELEKEEEREEDERIL---EYLKEKAE---REEEREAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1606 QVAAEKAIKQADediQGTQnlLTSIESETAASEETLtnasqriskLERNVEELKRKAAQNsgEAEYIEKvvysvKQNA-D 1684
Cdd:pfam13868 177 EIEEEKEREIAR---LRAQ--QEKAQDEKAERDELR---------AKLYQEEQERKERQK--EREEAEK-----KARQrQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1685 DVKKTLDGELDEKYKK-----------VESLIAQKTE----ESADARRKAELLQNEAKTLLAQANSKLQL-LEDLERKYE 1748
Cdd:pfam13868 236 ELQQAREEQIELKERRlaeeaereeeeFERMLRKQAEdeeiEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELE 315
|
330 340
....*....|....*....|....*.
gi 1666305206 1749 DNQKYLEDKAQELVRLEGEVRSLLKD 1774
Cdd:pfam13868 316 EGERLREEEAERRERIEEERQKKLKE 341
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1576-1736 |
5.60e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1576 EEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLltsieSETAASEEtltnasqriSKLERNV 1655
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL-----PKPADTSS---------PKEDKQV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 EELKRKAaqnsgeaeyIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANS 1735
Cdd:pfam05262 276 AENQKRE---------IEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
.
gi 1666305206 1736 K 1736
Cdd:pfam05262 347 Q 347
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1457-1745 |
6.17e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1457 EVEQLSKMVSEAKVR---ADEAKQNAQDVL---------LKTNATKEKVD----KSNEDLRNLIKQIrnfLTEDSADLDS 1520
Cdd:pfam05701 43 ELEKVQEEIPEYKKQseaAEAAKAQVLEELestkrlieeLKLNLERAQTEeaqaKQDSELAKLRVEE---MEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1521 IEAVAN-EVLKMEMPSTPQQLQNltedIRERVETLSQV-EVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEA 1598
Cdd:pfam05701 120 VAAKAQlEVAKARHAAAVAELKS----VKEELESLRKEyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKES 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1599 LE-------EAEKAQVAA-----------EKAIKQADEDIQGTQNLLTS---IESETAASEETLTN-----ASQRISKL- 1651
Cdd:pfam05701 196 LEsahaahlEAEEHRIGAalareqdklnwEKELKQAEEELQRLNQQLLSakdLKSKLETASALLLDlkaelAAYMESKLk 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1652 ERNVEELKRKAAQNSgeaeyIEKVVYSVKQNADDVKKTLDGELDE-KYKKV--ESLIAQKTEESADArrkAELLQNEAKT 1728
Cdd:pfam05701 276 EEADGEGNEKKTSTS-----IQAALASAKKELEEVKANIEKAKDEvNCLRVaaASLRSELEKEKAEL---ASLRQREGMA 347
|
330
....*....|....*..
gi 1666305206 1729 LLAQANsklqLLEDLER 1745
Cdd:pfam05701 348 SIAVSS----LEAELNR 360
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1539-1743 |
6.98e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1539 QLQNLTEDIRERVETLSQvevilQQSAADIARAELL----LEEAkrASKSATDVKVTADMVKEALEEAekAQVAAEKAIK 1614
Cdd:PRK09510 99 EQERLKQLEKERLAAQEQ-----KKQAEEAAKQAALkqkqAEEA--AAKAAAAAKAKAEAEAKRAAAA--AKKAAAEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1615 QADEDIQGTQNLLTSIESETAASEETltnasqrisklernVEELKRKAAQnsgEAEyiekvvysvKQNADDVKKTLDGEL 1694
Cdd:PRK09510 170 KAEAEAAKKAAAEAKKKAEAEAAAKA--------------AAEAKKKAEA---EAK---------KKAAAEAKKKAAAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1695 DEKYKKVEsliaqkteesADARRKAELLQNEAKTLLAQANSKLQLLEDL 1743
Cdd:PRK09510 224 KAAAAKAA----------AEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1546-1717 |
7.11e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1546 DIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQN 1625
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1626 LLtsieSETAASEETLTNAsqrisklERNVEELKRKAAQNSGEAEYIEK-VVYSVKQNADDVKKTLDGELDekykKVESL 1704
Cdd:pfam00529 132 LA----PIGGISRESLVTA-------GALVAQAQANLLATVAQLDQIYVqITQSAAENQAEVRSELSGAQL----QIAEA 196
|
170
....*....|...
gi 1666305206 1705 IAQKTEESADARR 1717
Cdd:pfam00529 197 EAELKLAKLDLER 209
|
|
| GARP |
pfam16731 |
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, ... |
1539-1731 |
7.39e-05 |
|
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, is one of a subset of major surface molecules on Trypanosoma species. They are all surface-orientated, immunodominant, and highly charged. GARP is interesting as ts expression coincides with the loss and gain of variant surface glycoprotein (VSG) molecules in the tsetse vector. It has an extended helical bundle structure that is homologous to the core surface structure of VSG, suggesting that it might replace the bloodstream VSG as the trypanosomes differentiate inside the tsetse vector after a blood-meal.
Pssm-ID: 435545 [Multi-domain] Cd Length: 192 Bit Score: 45.45 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1539 QLQNLTEDIRERVETLsqVEVILQQSAADIaRAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADE 1618
Cdd:pfam16731 12 QLRGLPDTVSSALETA--AAASSKAFKAKV-QAEEAVELAESAGLNDPKAKEAVTRAREAAVRATEAAEAAATAASNVEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1619 DiqgTQNLLTSIESETAASEETLtnasQRISKLERNVEELKRKAAQNSGEAEYIekVVYSVKQNADDVKKTLDGELDEKY 1698
Cdd:pfam16731 89 N---AANLASVAWAYVPSLDDGL----KKLAECGNADEDVREAAKKCTKTAENV--TAQSLTEALEGLRKLFDVKSAERL 159
|
170 180 190
....*....|....*....|....*....|...
gi 1666305206 1699 KKvesliaqkteESADARRKAELLQNEAKTLLA 1731
Cdd:pfam16731 160 RK----------ETVEAHEELKSLEKAVEEAVR 182
|
|
| ApoLp-III |
pfam07464 |
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ... |
1477-1631 |
7.76e-05 |
|
Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.
Pssm-ID: 462172 [Multi-domain] Cd Length: 143 Bit Score: 44.67 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1477 QNAQDVL--LKTNaTKEKVDKsnedLRNLIKQIRNFLTEDSADLDS--------IEAVANEvLKMEMPSTPQQLQNLTED 1546
Cdd:pfam07464 16 PSQQEVVetIKEN-TENLVDQ----LKQVQKSLQEELKKASGEAEEalkelntkIVETADK-LSEANPEVVQKANELQEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1547 IRERVETlsqvevilqqsaadiaraelLLEEAKRASKSatdVKvtadmvkealEEAEKAQVAAEKAIKQA-DEDIQGTQN 1625
Cdd:pfam07464 90 FQSGVQS--------------------LVTESQKLAKS---IS----------ENSQGATEKLQKATKQAyDDAVQAAQK 136
|
....*.
gi 1666305206 1626 LLTSIE 1631
Cdd:pfam07464 137 LANQLQ 142
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1292-1685 |
8.13e-05 |
|
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: 47.91 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1292 AESLDKTVKELAEQLEFIKNSDIQgaldsitkyfqmsleaekRVNASTTDPNSTV---EQSALTRDRVEDLMLERESPFK 1368
Cdd:pfam12128 111 ANNDFVKCETVAELGRFMKNAGIQ------------------RTNLLNTREYRSIiqnDRTLLGRERVELRSLARQFALC 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1369 EQqEEQARLLDELAGKLQS--LDLSAVAQMTCgtppgADCSESECGGPNCRTDEGEKKCGGPGCGGLV---TVAHSAWQK 1443
Cdd:pfam12128 173 DS-ESPLRHIDKIAKAMHSkeGKFRDVKSMIV-----AILEDDGVVPPKSRLNRQQVEHWIRDIQAIAgimKIRPEFTKL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1444 AMDFDRdVLSALAEVEQLSKMVSEAKvRADEAKQNAQDVLLK---------TNATKEKVDKSNEDLRNLIKQIRNflteD 1514
Cdd:pfam12128 247 QQEFNT-LESAELRLSHLHFGYKSDE-TLIASRQEERQETSAelnqllrtlDDQWKEKRDELNGELSAADAAVAK----D 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1515 SADLDSIEAVANEVLKMEMPSTPQQLQNLtEDIRERVETLSQVEVILQQSAADIARAELLLEeAKRASKSATDVKVTADM 1594
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVTAKYNRRR-SKIKEQNNRDIAGIKDK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1595 VKEALEEAEKaQVAAEKAIKQADE----DIQGTQNLLTSIESE---------------TAASEETLTNASQRISKLERNV 1655
Cdd:pfam12128 399 LAKIREARDR-QLAVAEDDLQALEselrEQLEAGKLEFNEEEYrlksrlgelklrlnqATATPELLLQLENFDERIERAR 477
|
410 420 430
....*....|....*....|....*....|.
gi 1666305206 1656 EEL-KRKAAQNSGEAEyiEKVVYSVKQNADD 1685
Cdd:pfam12128 478 EEQeAANAEVERLQSE--LRQARKRRDQASE 506
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1019 |
9.59e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1666305206 976 CQCHHniDTTDPEACDKETGRCLkCLYHTEGDHCQLCQYGYYGD 1019
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1565-1707 |
9.86e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 44.39 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1565 AADIARAELLLEEAKRASKSAT----DVKVTAD-MVKEALEEAEKaqvAAEKAIKQADEDiqgtqnlltsIESETAASEE 1639
Cdd:COG0711 37 ADGLAEAERAKEEAEAALAEYEeklaEARAEAAeIIAEARKEAEA---IAEEAKAEAEAE----------AERIIAQAEA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1640 TLTNASQRIsklernVEELKRKAAQNSGEAeyIEKVvysvkqnaddVKKTLDGELDEKYkkVESLIAQ 1707
Cdd:COG0711 104 EIEQERAKA------LAELRAEVADLAVAI--AEKI----------LGKELDAAAQAAL--VDRFIAE 151
|
|
| alph_xenorhab_B |
NF033927 |
alpha-xenorhabdolysin family binary toxin subunit B; |
1490-1732 |
1.05e-04 |
|
alpha-xenorhabdolysin family binary toxin subunit B;
Pssm-ID: 411488 [Multi-domain] Cd Length: 223 Bit Score: 45.70 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1490 KEKVDKSNEDLRNLIKQIRN-FLTEDSADLdsieavanevlkmempstPQQLQNLTEDIRERVETLSQVEVILQQSAADI 1568
Cdd:NF033927 6 IAALRKSAAKIANKLDDLSQiNLREATLDL------------------LAQLQEQIAELEAQIAALESKLNELAEDRKVI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1569 ARAELLLEEAKrasksatdvkvTADMVKEAL---EEAEKAQVA-AEKAI-KQAdedIQGTQNLLTSIESetAASEETLTN 1643
Cdd:NF033927 68 IEAIDLIEKYN-----------IADLFKDLLptaEEIDSLGLPpPEKDLvKAA---IERLKKLLGKISE--GLTYIDLVE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1644 A----SQRISKLERNVEELKRKAAQNSGEAEYIeKVVYSVkqnaDDVKKTLDGEldekYKKVE----SLIAQKTEESADA 1715
Cdd:NF033927 132 ArdklRDRINALLAESRTLDKDIKALAGKLEEL-TAIAAI----DEERATWVAE----ARKVEqaweSFLDQLTELTSDS 202
|
250
....*....|....*..
gi 1666305206 1716 RRkaellQNEAKTLLAQ 1732
Cdd:NF033927 203 AN-----LAQLITQLNG 214
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1474-1634 |
1.13e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 44.24 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1474 EAKQNAQDVLLKTNATKEKV--DKSNEDLRNLIK-QIRNFLTEDSADLDSI--EAV-ANEVLKMEMPSTPQQLQNLTEDI 1547
Cdd:cd13769 5 ELIQKAQEAINNLAQQVQKQlgLQNPEEVVNTLKeQSDNFANNLQEVSSSLkeEAKkKQGEVEEAWNEFKTKLSETVPEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1548 RERVETLSQVEVILQQSAADIaraELLLEEAKrasKSATDVKvtadmvkealEEAEKAQVAAEKAIKQA-DEDIQGTQNL 1626
Cdd:cd13769 85 RKSLPVEEKAQELQAKLQSGL---QTLVTESQ---KLAKAIS----------ENSQKAQEELQKATKQAyDIAVEAAQNL 148
|
....*...
gi 1666305206 1627 LTSIESET 1634
Cdd:cd13769 149 QNQLQTAT 156
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1517-1743 |
1.16e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1517 DLDSIEAVANEvLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSAtdvKVTADMVK 1596
Cdd:TIGR02794 44 DPGAVAQQANR-IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAA---KQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1597 EALE-------------EAEKAQVAAEKAIKQADEDiqgtqnlltsiesetAASEEtltnasQRISKLERnvEELKRKAA 1663
Cdd:TIGR02794 120 QAEEakakqaaeakakaEAEAERKAKEEAAKQAEEE---------------AKAKA------AAEAKKKA--EEAKKKAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1664 QNSGEAEYIEKvvysvKQNADDVKktldgeldekyKKVEsliAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDL 1743
Cdd:TIGR02794 177 AEAKAKAEAEA-----KAKAEEAK-----------AKAE---AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDI 237
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1578-1770 |
1.33e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1578 AKRASKSATDVKVTADMV----KEALEEAEKAQVAAEkaikQADEdiqgtqnlltsiesetaaSEETLTNASQRISKLER 1653
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTdlkeRESQEDAKRAQQLKE----ELDK------------------KQIDADKAQQKADFAQD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1654 NVEELKRKAAQNSGEAEYIEKvvySVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADAR-RKAELLQNEAKtllaq 1732
Cdd:pfam05262 242 NADKQRDEVRQKQQEAKNLPK---PADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKdHKAFDLKQESK----- 313
|
170 180 190
....*....|....*....|....*....|....*...
gi 1666305206 1733 ANSKLQlledlERKYEDNQKYLEDKAQELVRLEGEVRS 1770
Cdd:pfam05262 314 ASEKEA-----EDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1570-1733 |
1.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1570 RAELLLEEAKRASKSATDVKVTadmvkEALEEAEKAQVAAEKAIKQADEDIQGTQN--------------LLTSIESETA 1635
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALL-----EAKEEIHKLRNEFEKELRERRNELQKLEKrllqkeenldrkleLLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1636 ASEETLTNASQRISKLERNVEELKRKAAQnsgEAEYIEKVvysvkqNADDVKKTLDGELDEKYKKVESLIAQKTEEsaDA 1715
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQ---ELERISGL------TAEEAKEILLEKVEEEARHEAAVLIKEIEE--EA 182
|
170
....*....|....*...
gi 1666305206 1716 RRKAEllqNEAKTLLAQA 1733
Cdd:PRK12704 183 KEEAD---KKAKEILAQA 197
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1632-1777 |
1.36e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1632 SETAASEETLTNASQRISKLERNVEELKRK----AAQNSGEAEYIEKVVYSVKQNADDVKKTLDgELDEKYKKVESLIAQ 1707
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrdelNEELKELAEKRDELNAQVKELREEAQELRE-KRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 1708 KTEESADARRKAELLqNEAKTLLAQANSKLQLLEDLERKYEDnqkyLEDKAQ-ELVRLEGEvRSLLKDISE 1777
Cdd:COG1340 80 RDELNEKLNELREEL-DELRKELAELNKAGGSIDKLRKEIER----LEWRQQtEVLSPEEE-KELVEKIKE 144
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1538-1777 |
1.39e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLteDIRERVETLSQVEVILQqsaadiarAELLLEEAKRASKSATDVKVTAdmVKEALEEAEKAQ-----VAAEKA 1612
Cdd:PRK04778 39 QELENL--PVNDELEKVKKLNLTGQ--------SEEKFEEWRQKWDEIVTNSLPD--IEEQLFEAEELNdkfrfRKAKHE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1613 IKQADEDIQGTQNLLTSIESEtaaseetltnasqrisklernVEELKRKAAQNSGEAEyiekvvySVKQNADDVKKTLDG 1692
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEE---------------------LQELLESEEKNREEVE-------QLKDLYRELRKSLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ----------ELDEKYKKVESLIAQKTEESAD-----ARR-----KAELLQNEAKT-----LLAQANSKL-QLLEDLERK 1746
Cdd:PRK04778 159 nrfsfgpaldELEKQLENLEEEFSQFVELTESgdyveAREildqlEEELAALEQIMeeipeLLKELQTELpDQLQELKAG 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1666305206 1747 YED--NQKY-LEDKA--QELVRLEGEVRSLLKDISE 1777
Cdd:PRK04778 239 YRElvEEGYhLDHLDieKEIQDLKEQIDENLALLEE 274
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1644-1778 |
1.42e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1644 ASQRISKLERNVEELKrKAAQNsgEAEYIEK-VVYSVKQNADDVKKTLDGELDEK---YKKVESLIAQKtEESADarRKA 1719
Cdd:PRK12704 29 AEAKIKEAEEEAKRIL-EEAKK--EAEAIKKeALLEAKEEIHKLRNEFEKELRERrneLQKLEKRLLQK-EENLD--RKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1720 ELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEG----EVRS-LLKDISEK 1778
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGltaeEAKEiLLEKVEEE 166
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1564-1669 |
1.53e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 46.40 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1564 SAADIARAELLLEEAKRASKSATDVKVTADM-------VKEALEEAEKAQVAAEKAIKQADEDIQGtqnlltsiesetAA 1636
Cdd:PRK12472 185 LAAAPARAETLAREAEDAARAADEAKTAAAAaareaapLKASLRKLERAKARADAELKRADKALAA------------AK 252
|
90 100 110
....*....|....*....|....*....|...
gi 1666305206 1637 SEETLTNAsqrisklernvEELKRKAAQNSGEA 1669
Cdd:PRK12472 253 TDEAKARA-----------EERQQKAAQQAAEA 274
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
1538-1657 |
1.54e-04 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 43.24 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSaTDVKV--TAD-MVKEALEEAEK------AQVA 1608
Cdd:cd23160 3 QRLLAELQQLEQQAEALQQQIELLQASINELNRAKETLEELKKLKEG-TEILVpiGGGsFVKAKIKDTDKvlvnigAGVV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1666305206 1609 AEKAIKQADEDIqgtQNLLTSIESETAASEETLTNASQRISKLERNVEE 1657
Cdd:cd23160 82 VEKTIDEAIEIL---EKRIKELEKALEKLQEQLQQIAQRLEELEAELQE 127
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1547-1759 |
1.63e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.18 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1547 IRERVETLSQVEVILQQSAADIARaelllEEAKRASKsatDVKVTADMVKEALEEA-EKAQVAAEKAIKQADEDIQGTQN 1625
Cdd:pfam01442 2 LEDSLDELSTYAEELQEQLGPVAQ-----ELVDRLEK---ETEALRERLQKDLEEVrAKLEPYLEELQAKLGQNVEELRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1626 LLTSIESETAAseetltnasqrisKLERNVEELKRKAAQNSGEAEyiEKvvysVKQNADDVKKTLDGELDEkykkveslI 1705
Cdd:pfam01442 74 RLEPYTEELRK-------------RLNADAEELQEKLAPYGEELR--ER----LEQNVDALRARLAPYAEE--------L 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1706 AQKTEESADARRkaELLQNEAKTLLAQANSKLQlleDLERKYEDNQKYLEDKAQ 1759
Cdd:pfam01442 127 RQKLAERLEELK--ESLAPYAEEVQAQLSQRLQ---ELREKLEPQAEDLREKLD 175
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1467-1779 |
1.71e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.75 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1467 EAKVRADEAKQNAQDVLLKTNATK--EKVDKSNEDLRNLIKQIRNflTEDSADLDSIEAVANEVLKM--EMPSTPQQL-- 1540
Cdd:PTZ00440 190 DEKFNEYKNKKEAFYNCLKNKKEDydKKIKKINNEIRKLLKNIKC--TGNMCKTDTYVDMVELYLLRvnEVPSNNYDNyl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1541 ----------QNLTEDIRERVE---TLSQVEVILQQSAADIARAELLL-------EEAKRASKSATDVKVTADMVK---- 1596
Cdd:PTZ00440 268 nrakellesgSDLINKIKKELGdnkTIYSINFIQEEIGDIIKRYNFHLkkiekgkEYIKRIQNNNIPPQVKKDELKkkyf 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1597 -------------EALEEAEKAQVAAEKA-----------IKQADEDIQGTQNLLTSIESETAASEETLTNA-------S 1645
Cdd:PTZ00440 348 esakhyasfkfslEMLSMLDSLLIKKEKIlnnlfnklfgdLKEKIETLLDSEYFISKYTNIISLSEHTLKAAedvlkenS 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1646 QRISKLERN----VEELKRKAAQNSGEaeyIEKVVYSVKQNADDVKKTLDGELDEKyKKVESLIAQKTEESADARRKAEL 1721
Cdd:PTZ00440 428 QKIADYALYsnleIIEIKKKYDEKINE---LKKSINQLKTLISIMKSFYDLIISEK-DSMDSKEKKESSDSNYQEKVDEL 503
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1722 LQ--NEAKTLLAQANSKLQlleDLERKYED-------------NQKYLEDKAQELVRLEGEVRSLLKDISEKV 1779
Cdd:PTZ00440 504 LQiiNSIKEKNNIVNNNFK---NIEDYYITieglkneieglieLIKYYLQSIETLIKDEKLKRSMKNDIKNKI 573
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1540-1636 |
2.04e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.07 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1540 LQNLTEDIRERVE-TLSQVEVILQQSAADIARAELLLEEAK-RASKSATDVKVTADMVKEALEEAekAQVAAEKAIKQAD 1617
Cdd:pfam00430 24 LGKVLDKRRELIAdEIAEAEERRKDAAAALAEAEQQLKEARaEAQEIIENAKKRAEKLKEEIVAA--AEAEAERIIEQAA 101
|
90 100
....*....|....*....|
gi 1666305206 1618 EDI-QGTQNLLTSIESETAA 1636
Cdd:pfam00430 102 AEIeQEKDRALAELRQQVVA 121
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1217-1604 |
2.26e-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: 46.00 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1217 RETVDSVEKKVNEI-KDILAQS----PAAEP----LKNIGILFEEAEKLT--------KDVTEKMAQvevkltdtasqsn 1279
Cdd:pfam06160 120 REEVEELKDKYRELrKTLLANRfsygPAIDElekqLAEIEEEFSQFEELTesgdyleaREVLEKLEE------------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1280 stagELGALQAEAES----LDKTVKELAEQLEFIKN--------------SDIQGALDSITKYFQMSLEAEKRvnastTD 1341
Cdd:pfam06160 187 ----ETDALEELMEDipplYEELKTELPDQLEELKEgyremeeegyalehLNVDKEIQQLEEQLEENLALLEN-----LE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1342 PNSTVEQSALTRDRVEDL--MLERES----PFKEQQEEQARLLDELAGKLQSL--DLSAVAQmtcgtppgadcsesecgg 1413
Cdd:pfam06160 258 LDEAEEALEEIEERIDQLydLLEKEVdakkYVEKNLPEIEDYLEHAEEQNKELkeELERVQQ------------------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1414 pNCRTDEGEKKCGGPGCGGLVTV--AHSAWQKAMDFDRDVLSALAE--------VEQLSKMVSE-----AKVRADE--AK 1476
Cdd:pfam06160 320 -SYTLNENELERVRGLEKQLEELekRYDEIVERLEEKEVAYSELQEeleeileqLEEIEEEQEEfkeslQSLRKDEleAR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1477 QNAQDVLLKTNATKEKVDKSNedLRNLIKQIRNFLTEDSadlDSIEAVANEV--LKMEMPstpqQLQNLTEDIRERVETL 1554
Cdd:pfam06160 399 EKLDEFKLELREIKRLVEKSN--LPGLPESYLDYFFDVS---DEIEDLADELneVPLNMD----EVNRLLDEAQDDVDTL 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1666305206 1555 -SQVEVILQQSAAdiarAELLLEEAKR-ASKSATdvkvtadmVKEALEEAEK 1604
Cdd:pfam06160 470 yEKTEELIDNATL----AEQLIQYANRyRSSNPE--------VAEALTEAEL 509
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1581-1778 |
3.09e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 ASKSATDVkVTADMVKEALEEAEKA--QVAAEKAIKQadeDIQGTQNLLTSIE---SETAASEETLTNASQRISKLERNV 1655
Cdd:PRK11281 28 RAASNGDL-PTEADVQAQLDALNKQklLEAEDKLVQQ---DLEQTLALLDKIDrqkEETEQLKQQLAQAPAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1656 EELKRKAAQNSGEA------EYIEKVVYSVKQNADDVKKTLDG-----------------ELDEKYKKVESLIAQ----- 1707
Cdd:PRK11281 104 EALKDDNDEETRETlstlslRQLESRLAQTLDQLQNAQNDLAEynsqlvslqtqperaqaALYANSQRLQQIRNLlkggk 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1708 --KTEESADARRK--AEL----LQNEAKTLLAQANSKLQLLEDLERKYednqkyledKAQELVRLEGEVRSLLKDISEK 1778
Cdd:PRK11281 184 vgGKALRPSQRVLlqAEQallnAQNDLQRKSLEGNTQLQDLLQKQRDY---------LTARIQRLEHQLQLLQEAINSK 253
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1688-1779 |
3.16e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 43.29 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1688 KTLDGELDEKYKKVESLIAQKteeSADARRKAELLQNEAKTLLAQANSKLQllEDLERKYEDNQKYLEDKAQELVRLEGE 1767
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKL---EKELQALQEKLQKEAATLSEEERQKKE--RELQKKQQELQRKQQEAQQDLQKRQQE 116
|
90
....*....|..
gi 1666305206 1768 vrsLLKDISEKV 1779
Cdd:COG2825 117 ---LLQPILEKI 125
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1241-1307 |
4.60e-04 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 40.42 E-value: 4.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1241 EPLKNIGilfEEAEKLTKDVTEKMAQVEV---KLTDTASQSNSTAGELGALQAEAESLDktvKELAEQLE 1307
Cdd:cd22301 2 ERLKNIK---KEAENLAKEIEDKMKRIEDlekRIQDLNKRKEDKANQLARLEKQVISLR---KEIVERVE 65
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1630-1777 |
4.62e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1630 IESETAASEETLTNASQRISKLERNVE---ELKRKAAQNSGEAeYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIA 1706
Cdd:PRK00106 26 MKSAKEAAELTLLNAEQEAVNLRGKAErdaEHIKKTAKRESKA-LKKELLLEAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1666305206 1707 QKTEESADARRKAELLqneaktllaqaNSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:PRK00106 105 RLTERATSLDRKDENL-----------SSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAA 164
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1449-1780 |
4.66e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1449 RDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVllktNATKEKVDKSNEDLRNLIKQIrnfltedsADLDSIEAvanev 1528
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQI--------ADDEKSHS----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1529 lkmempstpqqlqnltedirervetlsqvevilqqsaadiaraeLLLEEAKRASKSATDVKVTADMVKEALEEAEkaqvA 1608
Cdd:PRK01156 215 --------------------------------------------ITLKEIERLSIEYNNAMDDYNNLKSALNELS----S 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1609 AEKAIKQADEDIQGTQNLLTSIESETAaseeTLTNASQRISKLERNVEELKRkaaqnsgeaEYIEKVVYSVKQ--NADDV 1686
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNN----YYKELEERHMKIINDPVYKNR---------NYINDYFKYKNDieNKKQI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1687 KKTLDGEL---DEKYKKVESLIAQKTEESADARRKAEL--LQNEAKTLLAQANSKLQLLEDLERK---YEDNQKYLEDK- 1757
Cdd:PRK01156 314 LSNIDAEInkyHAIIKKLSVLQKDYNDYIKKKSRYDDLnnQILELEGYEMDYNSYLKSIESLKKKieeYSKNIERMSAFi 393
|
330 340 350
....*....|....*....|....*....|...
gi 1666305206 1758 ----------AQELVRLEGEVRSLLKDISEKVA 1780
Cdd:PRK01156 394 seilkiqeidPDAIKKELNEINVKLQDISSKVS 426
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1538-1784 |
4.98e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLSQVEVILQQSAADIARAELL---LEEAKRAsksatdvkvtadmvkeALEEAEKAQVAAEKAI- 1613
Cdd:COG0497 155 ELLEEYREAYRAWRALKKELEELRADEAERARELDLLrfqLEELEAA----------------ALQPGEEEELEEERRRl 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1614 KQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERnveelkrkaaqnsgeaeyiekvvysvkqnaddvkktLDGE 1693
Cdd:COG0497 219 SNAEKLREALQEALEALSGGEGGALDLLGQALRALERLAE------------------------------------YDPS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1694 LDEKYKKVESLIAQKTEESADARRKAELLQ-NEAKtlLAQANSKLQLLEDLERKY----EDNQKYLEDKAQELVRLEG-- 1766
Cdd:COG0497 263 LAELAERLESALIELEEAASELRRYLDSLEfDPER--LEEVEERLALLRRLARKYgvtvEELLAYAEELRAELAELENsd 340
|
250
....*....|....*....
gi 1666305206 1767 -EVRSLLKDISEKVAVYST 1784
Cdd:COG0497 341 eRLEELEAELAEAEAELLE 359
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1669-1775 |
5.44e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1669 AEYIEKVVYSVKQNADdvkktLDGELDEKYKKVESLIAQKTE----ESADARRKAELLQNEAKTLLAQANSKLQLLEDLE 1744
Cdd:pfam00038 14 ASYIDKVRFLEQQNKL-----LETKISELRQKKGAEPSRLYSlyekEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1666305206 1745 RKYEDNQ--------------KYLEDKAQELVRLEGEVRSLLKDI 1775
Cdd:pfam00038 89 QKYEDELnlrtsaendlvglrKDLDEATLARVDLEAKIESLKEEL 133
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1541-1780 |
5.52e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1541 QNLTEDIRERVETLSQVEVILQ---QSAAD--------------IARAELLLEEAKRASKSATDVkvtadmVKEALEEAE 1603
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDLEqdyQAASDhlnlvqtalrqqekIERYQADLEELEERLEEQNEV------VEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1604 KAQVAAEKAIKQADE------------DIQGT--------QNLLTSIESETAASEETLTNASQRISKLERNVEE------ 1657
Cdd:PRK04863 380 ENEARAEAAEEEVDElksqladyqqalDVQQTraiqyqqaVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEateell 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1658 -LKRKAAQNSGEAEYIEKVVYSVKQNADDVkktldgELDEKYKKVESLIAQKTEESADARRkAELLQNEAKTL---LAQA 1733
Cdd:PRK04863 460 sLEQKLSVAQAAHSQFEQAYQLVRKIAGEV------SRSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELeqrLRQQ 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1666305206 1734 NSKLQLLEDLERKYEDNqkylEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:PRK04863 533 QRAERLLAEFCKRLGKN----LDDEDELEQLQEELEARLESLSESVS 575
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1611-1769 |
6.10e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1611 KAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLER---NVEELKRKAAQNSGEAeyIEKVVYSVKQN--ADD 1685
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRriqLLEEELERTEERLAEA--LEKLEEAEKAAdeSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1686 VKKTLDGELDEKYKKVESLIAQKTEesadarrkAELLQNEAKTLLAQANSKLQLLE-DLERKyEDNQKYLEDKAQElvrL 1764
Cdd:pfam00261 79 GRKVLENRALKDEEKMEILEAQLKE--------AKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE---L 146
|
....*
gi 1666305206 1765 EGEVR 1769
Cdd:pfam00261 147 EEELK 151
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1440-1734 |
6.25e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 44.26 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1440 AWQKAMDFDRDVLSALAEVEQlskmvseAKVRADEAKQNA---QDVLL------KTNATKEKVDKSNEDLRNLIKQIRNF 1510
Cdd:COG1538 5 LIERALANNPDLRAARARVEA-------ARAQLRQARAGLlpsQELDLggkrraRIEAAKAQAEAAEADLRAARLDLAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1511 LTE---DSADLDSIEAVANEVLKmempstpqQLQNLTEDIRERVET-------LSQVEVILQQSAADIARAELLLEEAKR 1580
Cdd:COG1538 78 VAQayfDLLAAQEQLALAEENLA--------LAEELLELARARYEAglasrldVLQAEAQLAQARAQLAQAEAQLAQARN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 A------SKSATDVKVTADMVKEALEEAEKAQV------------AAEKAIKQADEDI-------------------QGT 1623
Cdd:COG1538 150 AlalllgLPPPAPLDLPDPLPPLPPLPPSLPGLpsealerrpdlrAAEAQLEAAEAEIgvaraaflpslslsasygySSS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1624 QNLLTSIESETAASeetlTNASQRISKLERNVEELKR-KAAQNSGEAEYiEKVVYSVKQNADDVKKTLDgELDEKYKKVE 1702
Cdd:COG1538 230 DDLFSGGSDTWSVG----LSLSLPLFDGGRNRARVRAaKAQLEQAEAQY-EQTVLQALQEVEDALAALR-AAREQLEALE 303
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1666305206 1703 SLI--AQKTEESADARRKA------ELLQNEAKTLLAQAN 1734
Cdd:COG1538 304 EALeaAEEALELARARYRAglasllDVLDAQRELLQAQLN 343
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1569-1618 |
7.35e-04 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 39.67 E-value: 7.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1569 ARAELLLEEAKRASKSATDVKVTADmvkEALEEAEKAQVAAEKAIKQADE 1618
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAD---EAAARANAAEAAAEEAQQAAEE 54
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1659 |
8.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1247 GILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEfiknsdiqgaldsitkyfq 1326
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1327 mslEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQ--EEQARLLDELAGKLQSLDLSAVAQMtcgtppga 1404
Cdd:COG4372 84 ---ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdlEQQRKQLEAQIAELQSEIAEREEEL-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1405 dcsesecggpncrtdegekkcggpgcgglvtvahSAWQKAMDFDRDVLSALaEVEQLSKMVSEAKVRADEAKQNAQDVLL 1484
Cdd:COG4372 153 ----------------------------------KELEEQLESLQEELAAL-EQELQALSEAEAEQALDELLKEANRNAE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1485 KTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDsIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQS 1564
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG-LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1565 AADIARAELLLEEAKRASKSATDVKVTADMVkEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNA 1644
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAAL-SLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
410
....*....|....*
gi 1666305206 1645 SQRISKLERNVEELK 1659
Cdd:COG4372 356 LELLSKGAEAGVADG 370
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1538-1745 |
8.94e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 43.04 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLS----QVEVILQQSAADIARAellleeakrasksatdvkvtADMVKEALEEAEKAQVAAEKAI 1613
Cdd:smart00283 7 EEIAAGAEEQAEELEELAermeELSASIEEVAANADEI--------------------AATAQSAAEAAEEGREAVEDAI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1614 KQADEdiqgtqnlLTSIESETAASEETLTNASQRISKLernVEELKRKAAQ------NSGeaeyIE-----------KVV 1676
Cdd:smart00283 67 TAMDQ--------IREVVEEAVSAVEELEESSDEIGEI---VSVIDDIADQtnllalNAA----IEaarageagrgfAVV 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1677 ysvkqnADDVKKtLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLER 1745
Cdd:smart00283 132 ------ADEVRK-LAERSAESAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVD 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1538-1717 |
1.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1538 QQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSatdvkvtadmvkEALEEAEKAQVAAEKAIKQAD 1617
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG------------DRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1618 EDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEyiekvvysvkqnadDVKKTLDGELDEK 1697
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE--------------AALRDLRRELREL 424
|
170 180
....*....|....*....|...
gi 1666305206 1698 YKKVESLIAQKT---EESADARR 1717
Cdd:COG4913 425 EAEIASLERRKSnipARLLALRD 447
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1251-1396 |
1.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1251 EEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEfIKNSDI---QGALDSITKYFQM 1327
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIeerREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1328 SLEAEKRVNA--STTDPNSTVEQ-SALTR------DRVEDLMLERESP------FKEQQEEQARLLDELAGKLQSLDlSA 1392
Cdd:COG3883 98 SGGSVSYLDVllGSESFSDFLDRlSALSKiadadaDLLEELKADKAELeakkaeLEAKLAELEALKAELEAAKAELE-AQ 176
|
....
gi 1666305206 1393 VAQM 1396
Cdd:COG3883 177 QAEQ 180
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1561-1706 |
1.09e-03 |
|
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: 43.13 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1561 LQQSAADIARA--ELLLEEAKRASKSATDvkvtaDMVKEAleeaEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:cd22656 96 ILELIDDLADAtdDEELEEAKKTIKALLD-----DLLKEA----KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1639 ETLTNASQRISKLErnVEELKRKAAQNsgEAEYIEKvvysVKQNADDVKKTLDgELDEKYKKVESLIA 1706
Cdd:cd22656 167 DLLTDEGGAIARKE--IKDLQKELEKL--NEEYAAK----LKAKIDELKALIA-DDEAKLAAALRLIA 225
|
|
| DivIVA |
pfam05103 |
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ... |
1670-1752 |
1.14e-03 |
|
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.
Pssm-ID: 428304 [Multi-domain] Cd Length: 131 Bit Score: 41.01 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1670 EYIEKVVYS----VKQNAD--DVKKTLDGELDEkYKKVE-----SLI-AQKT-EES-ADARRKAELLQNEA----KTLLA 1731
Cdd:pfam05103 25 EFLDQVAEDyealIRENAElkEKIEELEEKLAH-YKNLEetlqnTLIlAQETaEEVkANAQKEAELIIKEAeakaERIVD 103
|
90 100
....*....|....*....|.
gi 1666305206 1732 QANSKLQlleDLERKYEDNQK 1752
Cdd:pfam05103 104 DANNEVK---KINDEIEELKR 121
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1456-1778 |
1.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1456 AEVEQLSKMVSEAK--VRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNfLTEDSADLDSIEavanevlkmem 1533
Cdd:COG4913 624 EELAEAEERLEALEaeLDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALE----------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1534 pstpQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTAD------MVKEALEEAEKAQV 1607
Cdd:COG4913 692 ----EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleeRFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1608 AA--EKAIKQADEDIQG-------------------TQNLLTSIES--ETAA-----SEETLTNASQRISKL-----ERN 1654
Cdd:COG4913 768 REnlEERIDALRARLNRaeeeleramrafnrewpaeTADLDADLESlpEYLAlldrlEEDGLPEYEERFKELlnensIEF 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1655 VEELKRKAAQNSGEA-EYIEKVVYSVKQ---NAD-----DVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNE 1725
Cdd:COG4913 848 VADLLSKLRRAIREIkERIDPLNDSLKRipfGPGrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKR 927
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1726 AKTLLAqANSKLQLLEDLERkYEDNQKYLEDKAQELVRLEGEVRSLLKDISEK 1778
Cdd:COG4913 928 LIERLR-SEEEESDRRWRAR-VLDVRNHLEFDAEEIDREDGEEVETYSSSGGK 978
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1572-1783 |
1.29e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1572 ELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKA-IKQADEDIQGTQNLLTSIESETAASEETLTNASQRISK 1650
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVsVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1651 LERNVEELKRKAA-----QNSGEAEYIEKVVYSVKQNADDVKKTLDG-----ELDEKYKKVESLIAQKTEESADAR---R 1717
Cdd:PRK05771 119 LEQEIERLEPWGNfdldlSLLLGFKYVSVFVGTVPEDKLEELKLESDvenveYISTDKGYVYVVVVVLKELSDEVEeelK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1718 KAELLQNEA---KTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYS 1783
Cdd:PRK05771 199 KLGFERLELeeeGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALS 267
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1218-1388 |
1.29e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1218 ETVDSVEKKVNEIKDILAqsPAAEPLknIGILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNST-AGELGALQAEAESL- 1295
Cdd:pfam01442 4 DSLDELSTYAEELQEQLG--PVAQEL--VDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKlGQNVEELRQRLEPYt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1296 DKTVKELAEQLEfiknsDIQGALDSITKyfqmslEAEKRVNASTTdpnSTVEQSALTRDRVEDLMLERESPFKEQQEEQA 1375
Cdd:pfam01442 80 EELRKRLNADAE-----ELQEKLAPYGE------ELRERLEQNVD---ALRARLAPYAEELRQKLAERLEELKESLAPYA 145
|
170
....*....|....
gi 1666305206 1376 -RLLDELAGKLQSL 1388
Cdd:pfam01442 146 eEVQAQLSQRLQEL 159
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1679-1778 |
1.31e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1679 VKQNADDVKKTLDgeldekykKVESLIAQKTEESADARRKAELL----QNEAKTL----LAQANSKLQlledleRKYEDN 1750
Cdd:PRK07353 41 IRTNRAEAKERLA--------EAEKLEAQYEQQLASARKQAQAViaeaEAEADKLaaeaLAEAQAEAQ------ASKEKA 106
|
90 100
....*....|....*....|....*....
gi 1666305206 1751 QKYLEDKAQE-LVRLEGEVRSLLKDISEK 1778
Cdd:PRK07353 107 RREIEQQKQAaLAQLEQQVDALSRQILEK 135
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1454-1664 |
1.47e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1454 ALAEVEQLSKM-VSEAKVRADEAK-QNAQDVLLKTNATKEKvdksneDLRnlIKQIRNFLTEDSADLDSIEAVANEVLKM 1531
Cdd:COG2268 204 AEAEAERETEIaIAQANREAEEAElEQEREIETARIAEAEA------ELA--KKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1532 EmpstpQQLQNLTEDIRErvetlsQVEVILQQSAADIARAELLLEEAKRASKSATdvkvtadmVKEALEEAEkAQVAAEK 1611
Cdd:COG2268 276 E-----REVQRQLEIAER------EREIELQEKEAEREEAELEADVRKPAEAEKQ--------AAEAEAEAE-AEAIRAK 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1666305206 1612 AIKQAdediQGTQNLltsiesetAASEETLTNAsQRISKLERNVEELKRKAAQ 1664
Cdd:COG2268 336 GLAEA----EGKRAL--------AEAWNKLGDA-AILLMLIEKLPEIAEAAAK 375
|
|
| PhaF |
COG3937 |
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport ... |
1568-1661 |
1.50e-03 |
|
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms];
Pssm-ID: 443138 [Multi-domain] Cd Length: 103 Bit Score: 39.78 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1568 IARAELLLEEAKRasksatdvkvtadMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLltsiesetaASEETLTNASQR 1647
Cdd:COG3937 31 VEKGELTEEEAKK-------------FVDELVEKGEEEKEELEEKIEEQVEEALEKLGL---------ATKEEVDELEER 88
|
90
....*....|....
gi 1666305206 1648 ISKLERNVEELKRK 1661
Cdd:COG3937 89 IDRLEKQLRELENK 102
|
|
| GARP |
pfam16731 |
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, ... |
1451-1612 |
1.56e-03 |
|
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, is one of a subset of major surface molecules on Trypanosoma species. They are all surface-orientated, immunodominant, and highly charged. GARP is interesting as ts expression coincides with the loss and gain of variant surface glycoprotein (VSG) molecules in the tsetse vector. It has an extended helical bundle structure that is homologous to the core surface structure of VSG, suggesting that it might replace the bloodstream VSG as the trypanosomes differentiate inside the tsetse vector after a blood-meal.
Pssm-ID: 435545 [Multi-domain] Cd Length: 192 Bit Score: 41.59 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1451 VLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLI-------KQIRNfLTEDSADLDSIEA 1523
Cdd:pfam16731 20 VSSALETAAAASSKAFKAKVQAEEAVELAESAGLNDPKAKEAVTRAREAAVRATeaaeaaaTAASN-VEINAANLASVAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1524 VANEVLKMEMPSTPQQlQNLTEDIRERVETLSQV-EVILQQS---AADIARAELLLEEAKRASKSATDVKVTADMVKEAL 1599
Cdd:pfam16731 99 AYVPSLDDGLKKLAEC-GNADEDVREAAKKCTKTaENVTAQSlteALEGLRKLFDVKSAERLRKETVEAHEELKSLEKAV 177
|
170
....*....|...
gi 1666305206 1600 EEAEKAQVAAEKA 1612
Cdd:pfam16731 178 EEAVRAQKAAEDA 190
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1688-1779 |
1.70e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1688 KTLDGELDEKYKKVESLIAQKTEEsadARRKAELLQNEAKTLLAQANSKLQlleDLERKYEDNQKYLEDKAQELVRLEGE 1767
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE---LQKLYEELQKDGALLEEEREEKEQ---ELQKKEQELQQLQQKAQQELQKKQQE 91
|
90
....*....|..
gi 1666305206 1768 vrsLLKDISEKV 1779
Cdd:pfam03938 92 ---LLQPIQDKI 100
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-326 |
1.72e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1666305206 271 CFCYGHASECAPVDgvneevegMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEG 326
Cdd:pfam00053 1 CDCNPHGSLSDTCD--------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1647-1780 |
1.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1647 RISKLERNVEELKRKAAQNSGEAEYIEKVVySVKQNADDVKKTLDGELDEKYKKVESLiaqkTEESADARRKAELLQNEA 1726
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEI----SSELPELREELEKLEKEV 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1666305206 1727 KTLLAQANsKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVA 1780
Cdd:PRK03918 231 KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
1564-1682 |
1.91e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 40.93 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1564 SAADIARAEL---------LLEEAkRASKSAtdvkvtadMVKEALEEAEK--------AQVAAEKAIKQADEdiqgtqnl 1626
Cdd:PRK14471 49 ASAEEARKEMqnlqadnerLLKEA-RAERDA--------ILKEAREIKEKmiadakeeAQVEGDKMIEQAKA-------- 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1666305206 1627 ltSIESETAASEETLTN--ASQRISKLERNV-EELKRKAAQnsgeAEYIEKVVYSVKQN 1682
Cdd:PRK14471 112 --SIESEKNAAMAEIKNqvANLSVEIAEKVLrKELSNKEKQ----HKLVEKMLGDVKLN 164
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1453-1669 |
2.19e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1453 SALAEVEQLSKMVSEAKVRAD-----EAKQN-AQDVLLKTN--------ATKEKVDKSNEDLRNLIKQIRNFLTEDSADL 1518
Cdd:PRK11281 24 SAFARAASNGDLPTEADVQAQldalnKQKLLeAEDKLVQQDleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1519 DSIEAVANEVLKMEMPSTP-----QQLQNLTEDIRERVETLSQV--EVILQQSAADIARAElLLEEAKRaSKSATDVKVT 1591
Cdd:PRK11281 104 EALKDDNDEETRETLSTLSlrqleSRLAQTLDQLQNAQNDLAEYnsQLVSLQTQPERAQAA-LYANSQR-LQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1592 ADMVKEALEEAEKAQVAAEKAIKQADEDIQGT--------QNLLTSIESETAAseetltnasqRISKLERNVEEL----- 1658
Cdd:PRK11281 182 GKVGGKALRPSQRVLLQAEQALLNAQNDLQRKslegntqlQDLLQKQRDYLTA----------RIQRLEHQLQLLqeain 251
|
250 260
....*....|....*....|
gi 1666305206 1659 -KR--------KAAQNSGEA 1669
Cdd:PRK11281 252 sKRltlsektvQEAQSQDEA 271
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-966 |
2.19e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 917 CPCpdgpDSGRQFARSCyqDPVTLQlaCVCDPGYIGSRCDDCASGFFGNP 966
Cdd:smart00180 1 CDC----DPGGSASGTC--DPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1693-1780 |
2.55e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1693 ELDEKYKKVESLIAQKteeSADARRKAELLQNEAKTLLAQANSKLQllEDLERKYEDNQKYLEDKAQELVRLEGE----V 1768
Cdd:smart00935 22 QLEKEFKKRQAELEKL---EKELQKLKEKLQKDAATLSEAAREKKE--KELQKKVQEFQRKQQKLQQDLQKRQQEelqkI 96
|
90
....*....|..
gi 1666305206 1769 RSLLKDISEKVA 1780
Cdd:smart00935 97 LDKINKAIKEVA 108
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1648-1777 |
2.95e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1648 ISKLERNVEELKRKAAQNSgeaEYIEKVVySVKQNADDVKKTLDGELDEkYKKVESLIAQKTEESADArrkaelLQNEAK 1727
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLM---KELELLN-SIKPKLRDRKDALEEELRQ-LKQLEDELEDCDPTELDR------AKEKLK 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1728 TLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISE 1777
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1440-1705 |
4.02e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.93 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1440 AWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLD 1519
Cdd:COG0840 110 AALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1520 SIEAVANEVLKMEMPSTPQQLQNLTE--------DIRERVETLSQVEVilqqsaADIARA-ELLLEEAKRAsksATDVKV 1590
Cdd:COG0840 190 ALVALAIILALLLSRSITRPLRELLEvleriaegDLTVRIDVDSKDEI------GQLADAfNRMIENLREL---VGQVRE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1591 TADMVKEALEE-AEKAQVAAEKAIKQADediqgtqnlltSIEsETAASEETLTNASQRISKLERNVEELKRKAAQNSGEA 1669
Cdd:COG0840 261 SAEQVASASEElAASAEELAAGAEEQAA-----------SLE-ETAAAMEELSATVQEVAENAQQAAELAEEASELAEEG 328
|
250 260 270
....*....|....*....|....*....|....*....
gi 1666305206 1670 -EYIEKVVYSVKQNADDVKKTLD--GELDEKYKKVESLI 1705
Cdd:COG0840 329 gEVVEEAVEGIEEIRESVEETAEtiEELGESSQEIGEIV 367
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1610-1777 |
4.22e-03 |
|
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: 41.76 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1610 EKAIKQADEDIQG-----TQNLLTSIEsetaaseETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVK---- 1680
Cdd:pfam06160 66 EELLFEAEELNDKyrfkkAKKALDEIE-------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRktll 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1681 QNADDVKKTLDgELDEKYKKVESLIAQKTE--ESAD---ARRKAELLQNEAKTL----------LAQANSKL-QLLEDLE 1744
Cdd:pfam06160 139 ANRFSYGPAID-ELEKQLAEIEEEFSQFEEltESGDyleAREVLEKLEEETDALeelmedipplYEELKTELpDQLEELK 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 1666305206 1745 RKYED--NQKY-LEDK--AQELVRLEGEVRSLLKDISE 1777
Cdd:pfam06160 218 EGYREmeEEGYaLEHLnvDKEIQQLEEQLEENLALLEN 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1502-1742 |
4.94e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1502 NLIKQIRNFLTEDSADLDS-IEAVANEVLKMEmpstpQQLQNLtEDIRERVETLSQvEVILQQSAADIARAElLLEEAKR 1580
Cdd:PRK00409 502 NIIEEAKKLIGEDKEKLNElIASLEELERELE-----QKAEEA-EALLKEAEKLKE-ELEEKKEKLQEEEDK-LLEEAEK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1581 AsksatdvkvtadmVKEALEEAEKaqvAAEKAIKQADEDIQGTQnlltsieseTAASEETLTNASQRISKLERNVEELKR 1660
Cdd:PRK00409 574 E-------------AQQAIKEAKK---EADEIIKELRQLQKGGY---------ASVKAHELIEARKRLNKANEKKEKKKK 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1661 KAAQNSGEAEYIEKVVY-SVKQNADDVKKTLDGELDE---------KYKKVESLIAQKTEESADARRKAELLQNEAKTL- 1729
Cdd:PRK00409 629 KQKEKQEELKVGDEVKYlSLGQKGEVLSIPDDKEAIVqagimkmkvPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLELd 708
|
250
....*....|....*....
gi 1666305206 1730 -----LAQANSKL-QLLED 1742
Cdd:PRK00409 709 lrgmrYEEALERLdKYLDD 727
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1440-1611 |
5.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1440 AWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFltedSADLD 1519
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA----QEKAD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1520 SIEavanevlkmempstpQQLQNLTEDIRErvetlsqvevilqqsaadiaraelLLEEAKRASKSATDVKVTADmvKEAL 1599
Cdd:COG1340 227 ELH---------------EEIIELQKELRE------------------------LRKELKKLRKKQRALKREKE--KEEL 265
|
170
....*....|..
gi 1666305206 1600 EeaEKAQVAAEK 1611
Cdd:COG1340 266 E--EKAEEIFEK 275
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1589-1729 |
7.07e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.54 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1589 KVTADMVKEALEEAEK----AQVAAEKAIKQADEDIqgtQNLLTSIESETAASEETLTNasQRISKLERnveELKRK--A 1662
Cdd:COG1390 6 KIIEEILEEAEAEAEEileeAEEEAEKILEEAEEEA---EEIKEEILEKAEREAEREKR--RIISSAEL---EARKEllE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1663 AQNsgeaEYIEKVVYSVKQNADDVKKtldgelDEKYKK-VESLIAQKTEESADARRKAELLQNEAKTL 1729
Cdd:COG1390 78 AKE----ELIEEVFEEALEKLKNLPK------DPEYKElLKKLLKEAAEELGSGDLVVYVNEKDKELL 135
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1600-1774 |
7.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1600 EEAeKAQVAAEKaiKQADEDIQGTQNLltSIESETAASEetltnASQRISKLERNVEELKRKAAQNsgeAEYIEKVVYSV 1679
Cdd:PRK00409 505 EEA-KKLIGEDK--EKLNELIASLEEL--ERELEQKAEE-----AEALLKEAEKLKEELEEKKEKL---QEEEDKLLEEA 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1680 KQNADDVKKTLDGELDEKYKKVESLiaQKTEESADARRKAEllqnEAKTLLAQANSKLQlledlERKYEDNQKYLEDKAQ 1759
Cdd:PRK00409 572 EKEAQQAIKEAKKEADEIIKELRQL--QKGGYASVKAHELI----EARKRLNKANEKKE-----KKKKKQKEKQEELKVG 640
|
170 180
....*....|....*....|
gi 1666305206 1760 ELVRLE-----GEVRSLLKD 1774
Cdd:PRK00409 641 DEVKYLslgqkGEVLSIPDD 660
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1459-1672 |
8.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1459 EQLSKMVSEAKVRADEAKQNAqdvllKTNAtKEKVDKSNEDLRNLIKQIRNfltedsadldsieavanEVLKMEmpstpQ 1538
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEA-----LLEA-KEEIHKLRNEFEKELRERRN-----------------ELQKLE-----K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1666305206 1539 QLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKrasksatdvKVTADMVKEALEEAEK-AQVAAEKAIKQad 1617
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE---------EELEELIEEQLQELERiSGLTAEEAKEI-- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1666305206 1618 ediqgtqnLLTSIESEtaASEEtltnASQRISKLErnvEELKRKAAQnsgEAEYI 1672
Cdd:PRK12704 159 --------LLEKVEEE--ARHE----AAVLIKEIE---EEAKEEADK---KAKEI 193
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1707-1774 |
8.55e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 8.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1666305206 1707 QKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKaqelvrLEGEVRSLLKD 1774
Cdd:cd16269 195 EKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK------MEEERENLLKE 256
|
|
| |
